This is a working overview of mass spectrometry, written for readers who want more than a one-paragraph summary but less than a textbook.
Reviewed 2025-09-23. Anything still debated is marked as such rather than presented as settled.
Outside its country of origin the compound is generally handled as a research chemical rather than an approved medicine. No regulatory approval from the United States Food and Drug Administration or the European Medicines Agency has been granted for human use. Identity and purity are normally checked by reverse-phase high-performance liquid chromatography, with mass spectrometry used to confirm the molecular mass. Lyophilised material is stored cold and desiccated, and repeated freeze-thaw cycles are avoided.
Published work on this peptide almost always uses intranasal delivery, with drops or a spray applied to the nasal mucosa. Some animal experiments have used subcutaneous or intraperitoneal injection, and a smaller number have compared routes directly. Oral administration is not a focus of the literature, because short peptides of this size are broken down by digestive enzymes and cross intestinal barriers poorly. How much of an intranasal dose reaches the bloodstream intact in humans remains an open question.
Tuftsin, the parent structure, is a naturally occurring immunomodulatory tetrapeptide released from the Fc region of immunoglobulin G by spleen enzymes. Selank extends this four-residue sequence with three additional amino acids. The stated rationale is that the added tail slows enzymatic breakdown and may influence receptor interactions. How the full heptapeptide behaves at the molecular level is not firmly established, and proposed mechanisms often involve indirect modulation of neurotransmitter or immune signaling rather than a single defined target.
Selank is a synthetic heptapeptide developed in Russia. Its sequence is Thr-Lys-Pro-Arg-Pro-Gly-Pro, a seven-residue chain built around the natural tetrapeptide tuftsin. Researchers at the Institute of Molecular Genetics of the Russian Academy of Sciences first described the compound in the mid-1990s. The design combined the tuftsin core with an added Pro-Gly-Pro tail, a modification intended to extend the molecule's stability in biological fluids. Published work on the peptide has appeared mainly in Russian-language journals.
| Property | Value | Notes |
|---|---|---|
| Common route | Intranasal | Also injected in some animal work |
| Solubility class | Freely soluble in water | Solid form is hygroscopic |
| Typical storage | About -20 degrees Celsius | Keep desiccated and dark |
| Purity method | Reverse-phase HPLC | Reported as area percent |
| Confirmatory method | Mass spectrometry | Verifies expected molecular mass |
Lyophilized Selank, the dry powder form, is generally stored frozen at minus 20 degrees Celsius or colder for long-term keeping. The solid is hygroscopic and should stay sealed, dry, and protected from light. Once dissolved, the peptide is less stable and is usually held refrigerated at 2 to 8 degrees Celsius for short periods. Repeated freezing and thawing is avoided because it can promote aggregation and loss of activity. Buffers and pH choice also affect how long a solution remains usable.
Solubility behavior is a practical concern for handling. Selank dissolves readily in water and in common aqueous buffers, which simplifies preparation of working solutions. The choice of solvent, ionic strength, and pH can influence aggregation over time, particularly at higher concentrations. Aqueous solutions are typically sterile-filtered before use. Because stability depends on several variables, storage and handling notes should be treated as general guidance rather than fixed rules, and specific values are best confirmed against a certificate of analysis for each batch.
Characterization of Selank in a laboratory setting relies on standard peptide methods. Reverse-phase high-performance liquid chromatography separates the target from related impurities and provides a purity figure, commonly reported as 95 percent or higher. Mass spectrometry, typically electrospray ionization or matrix-assisted laser desorption, confirms the molecular mass and helps detect truncation or modification. Amino acid analysis can verify composition when a sequence-level check is needed. These techniques together establish identity and purity for a given lot.
Peptide bonds are vulnerable to protease attack, and Selank is no exception. Measured half-life in serum is short, on the order of minutes in several reports, which explains why intranasal administration is the common route described in the literature. Absorption across the nasal mucosa partially bypasses first-pass hepatic metabolism. Quantitative data on human bioavailability remain limited and are difficult to compare across studies.
Lyophilised material kept dry at minus 20 degrees Celsius or colder is the most stable form, and suppliers commonly state a shelf life of two years or more under those conditions. Once dissolved, degradation accelerates through hydrolysis and deamidation, particularly at alkaline pH or elevated temperature. Working solutions are usually divided into single-use aliquots to avoid repeated freeze-thaw cycles. The choice of reconstitution solvent affects both stability and the ionic strength of the final preparation.
Selank is a synthetic heptapeptide with the sequence Thr-Lys-Pro-Arg-Pro-Gly-Pro. It was designed at the Institute of Molecular Genetics of the Russian Academy of Sciences as a structural analogue of tuftsin, a naturally occurring tetrapeptide fragment of the immunoglobulin heavy chain. The added Pro-Gly-Pro tail was intended to slow enzymatic degradation and extend biological activity. In Russia it is registered as an anxiolytic nasal preparation, while regulators elsewhere have not approved it for clinical use.
Proposed mechanisms centre on modulation of the GABAergic system, with reports of altered expression of genes related to GABA-A receptor subunits and changed monoamine turnover. Some studies describe inhibition of enkephalinase, the enzyme that degrades endogenous enkephalins, which may prolong opioid peptide signalling. Effects on brain-derived neurotrophic factor and on cytokine expression have also been reported. These findings come largely from animal models and small human studies, and the precise primary target remains unresolved.
Published clinical evidence is limited. Most controlled trials were conducted in Russia, enrolled modest numbers of participants, and appeared in Russian-language journals, which restricts independent verification. Reported outcomes include lower anxiety scores, improved attention and memory measures, and changes in fatigue ratings. Reviews written in English note methodological limitations such as small samples and inconsistent endpoints. Whether the compound produces clinically meaningful benefit relative to established anxiolytics is therefore an open question rather than an established finding.
Selank is a hydrophilic peptide and dissolves readily in water and in aqueous buffers. The lyophilised powder is typically a white to off-white solid. Because short peptides are prone to hydrolysis and oxidation, handling benefits from limiting exposure to heat, moisture and strong light. Working solutions are commonly prepared in sterile water or saline, and repeated freeze-thaw cycles are avoided to reduce aggregation and loss of activity. These practices reflect general laboratory convention rather than published stability specifications.
Dry powder is normally held at -20 degrees Celsius or lower, in a sealed container with desiccant and protection from light. Reconstituted solutions are usually kept at 2 to 8 degrees Celsius for short periods and frozen for longer ones. Proline residues at several positions are generally associated with some resistance to peptidase attack, but chemical stability still declines at neutral to alkaline pH and at elevated temperature. Exact shelf-life figures are product-specific and are not standardised across suppliers.
Naturally occurring rhodium is composed of only one isotope, 103Rh. With a nuclear spin of -1/2, 103Rh is well-suited for nuclear magnetic resonance spectroscopic studies. With a particularly low nuclear dipole moment, 103Rh exhibits very low receptivity. The most stable radioisotopes are 101Rh with a half-life of 4.07 years, 102Rh with a half-life of 207 days, and 99Rh with a half-life of 16.1 days. Thirty-eight other radioisotopes have been characterized ranging from 90Rh to 128Rh; these have half-lives that are less than an hour except 100Rh (20.8 hours) and 105Rh (35.34 hours). Numerous meta states are also known, of which the most stable are 102mRh (3.742 years) and 101mRh (4.343 days). In isotopes lighter than 103Rh (the stable isotope), the primary decay mode is electron capture and the primary decay product is ruthenium. In isotopes heavier than 103Rh, the primary decay mode is beta emission and the primary product is palladium.
Blood smear to evaluate cell morphology Iron panel to evaluate for concurrent iron deficiency JAK2 mutation testing Serum erythropoeitin (EPO) levels Oxygen saturation (usually via pulse oximetry or blood gas tests) or oxygen dissociation tests
=== ICD-11 === Anorexia nervosa is classified under feeding or eating disorders in both the ICD-11 and the DSM-5. Like the DSM-5, the ICD-11 also distinguishes between a binge-purge pattern and a restricting pattern with further subcodes.
Southern Association, previously Class A1 (1936–1945) Texas League, previously Class A1 (1936–1942; idle for three seasons during World War II) The Texas League remained in Double-A for the next 75 years. During this time, there were limited changes to leagues at the Double-A level:
2.A.1 Major Facilitator superfamily (MFS), see also Lactose permease, Phosphate permease and Glucose transporter 2.A.2 The Glycoside-Pentoside-Hexuronide (GPH):Cation Symporter Family 2.A.3 The Amino Acid-Polyamine-Organocation (APC) Family 2.A.4 Cation diffusion facilitator (CDF) Family 2.A.5 Zinc (Zn2+)-Iron (Fe2+) Permease Family 2.A.6 Resistance-Nodulation-Cell Division Superfamily, see also SecDF protein-export membrane protein 2.A.7 The Drug/Metabolite Transporter (DMT) Superfamily 2.A.8 The Gluconate:H+ Symporter (GntP) Family 2.A.9 The Membrane Protein Insertase (YidC/Alb3/Oxa1) Family 2.A.10 The 2-Keto-3-Deoxygluconate Transporter (KdgT) Family 2.A.11 The Citrate-Mg2+:H+ (CitM) Citrate-Ca2+:H+ (CitH) Symporter (CitMHS) Family 2.A.12 ATP:ADP Antiporter Family 2.A.13 The C4-Dicarboxylate Uptake (Dcu) Family 2.A.14 Lactate Permease Family 2.A.15 The Betaine/Carnitine/Choline Transporter (BCCT) Family 2.A.16 Tellurite-resistance/Dicarboxylate Transporter Family 2.A.17 Proton-dependent Oligopeptide Transporter Family 2.A.18 The Amino Acid/Auxin Permease (AAAP) Family 2.A.19 The Ca2+:Cation Antiporter (CaCA) Family 2.A.20 The Inorganic Phosphate Transporter (PiT) Family 2.A.21 Solute:Sodium Symporter Family 2.A.22 The Neurotransmitter:Sodium Symporter Family 2.A.23 The Dicarboxylate/Amino Acid:Cation (Na+ or H+) Symporter (DAACS) Family 2.A.24 The 2-Hydroxycarboxylate Transporter (2-HCT) Family 2.A.25 Alanine or Glycine:Cation Symporter (AGCS) Family 2.A.26 The Branched Chain Amino Acid:Cation Symporter (LIVCS) Family 2.A.27 The Glutamate:Na+ Symporter (ESS) Family 2.A.28 Bile Acid:Na+ Symporter Family 2.A.29 Mitochondrial carrier Family 2.A.30 Cation-Chloride Cotransporter (CCC) Family 2.A.31 Anion Exchanger Family 2.A.32 The Silicon Transporter (Sit) Family 2.A.33 NhaA Na+:H+ Antiporter (NhaA) Family 2.A.34 The NhaB Na+:H+ Antiporter (NhaB) Family 2.A.35 The NhaC Na+:H+ Antiporter (NhaC) Family 2.A.36 Monovalent Cation:Proton Antiporter-1 (CPA1) Family 2.A.37 Monovalent Cation:Proton Antiporter-2 (CPA2) Family 2.A.38 K+ Transporter (Trk) Family 2.A.39 Nucleobase:Cation Symporter-1 (NCS1) Family 2.A.40 Nucleobase:Cation Symporter-2 (NCS2) Family 2.A.41 The Concentrative Nucleoside Transporter (CNT) Family 2.A.42 The Hydroxy/Aromatic Amino Acid Permease (HAAAP) Family 2.A.43 The Lysosomal Cystine Transporter (LCT) Family 2.A.45 Arsenite-Antimonite Efflux Family 2.A.46 The Benzoate:H+ Symporter (BenE) Family 2.A.47 Divalent Anion:Na+ Symporter (DASS) Family 2.A.48 The Reduced Folate Carrier (RFC) Family 2.A.49 Chloride Carrier/Channel (ClC) Family 2.A.50 The Glycerol Uptake (GUP) Family 2.A.51 The Chromate Ion Transporter (CHR) Family 2.A.52 The Ni2+-Co2+ Transporter (NiCoT) Family 2.A.53 Sulfate permease (SulP) Family 2.A.54 The Mitochondrial Tricarboxylate Carrier (MTC) Family 2.A.55 The Metal Ion (Mn2+-iron) Transporter (Nramp) Family 2.A.56 The Tripartite ATP-independent Periplasmic Transporter (TRAP-T) Family 2.A.57 The Equilibrative Nucleoside Transporter (ENT) Family 2.A.58 The Phosphate:Na+ Symporter (PNaS) Family 2.A.59 The Arsenical Resistance-3 (ACR3) Family 2.A.60 Organo Anion Transporter (OAT) Family 2.A.61 The C4-dicarboxylate Uptake C (DcuC) Family 2.A.62 The NhaD Na+:H+ Antiporter (NhaD) Family 2.A.63 The Monovalent Cation (K+ or Na+):Proton Antiporter-3 (CPA3) Family 2.A.64 Twin Arginine Targeting (Tat) Family 2.A.65 The Bilirubin Transporter (BRT) Family 2.A.66 The Multidrug/Oligosaccharidyl-lipid/Polysaccharide (MOP) Flippase Superfamily 2.A.67 The Oligopeptide Transporter (OPT) Family 2.A.68 The p-Aminobenzoyl-glutamate Transporter (AbgT) Family 2.A.69 The Auxin Efflux Carrier (AEC) Family 2.A.70 The Malonate:Na+ Symporter (MSS) Family 2.A.71 The Folate-Biopterin Transporter (FBT) Family 2.A.72 The K+ Uptake Permease (KUP) Family 2.A.73 The Short Chain Fatty Acid Uptake (AtoE) Family 2.A.74 The 4 TMS Multidrug Endosomal Transporter (MET) Family 2.A.75 The L-Lysine Exporter (LysE) Family 2.A.76 The Resistance to Homoserine/Threonine (RhtB) Family 2.A.77 The Cadmium Resistance (CadD) Family 2.A.78 The Branched Chain Amino Acid Exporter (LIV-E) Family 2.A.79 The Threonine/Serine Exporter (ThrE) Family 2.A.80 The Tricarboxylate Transporter (TTT) Family 2.A.81 The Aspartate:Alanine Exchanger (AAEx) Family 2.A.82 The Organic Solute Transporter (OST) Family 2.A.83 The Na+-dependent Bicarbonate Transporter (SBT) Family 2.A.84 The Chloroplast Maltose Exporter (MEX) Family 2.A.85 The Aromatic Acid Exporter (ArAE) Family 2.A.86 The Autoinducer-2 Exporter (AI-2E) Family (Formerly the PerM Family, TC #9.B.22) 2.A.87 The Prokaryotic Riboflavin Transporter (P-RFT) Family 2.A.88 Vitamin Uptake Transporter (VUT or ECF) Family 2.A.89 The Vacuolar Iron Transporter (VIT) Family 2.A.90 Vitamin A Receptor/Transporter (STRA6) Family 2.A.91 Mitochondrial tRNA Import Complex (M-RIC) (Formerly 9.C.8) 2.A.92 The Choline Transporter-like (CTL) Family 2.A.94 The Phosphate Permease (Pho1) Family 2.A.95 The 6TMS Neutral Amino Acid Transporter (NAAT) Family 2.A.96 The Acetate Uptake Transporter (AceTr) Family 2.A.97 The Mitochondrial Inner Membrane K+/H+ and Ca2+/H+ Exchanger (LetM1) Family 2.A.98 The Putative Sulfate Exporter (PSE) Family 2.A.99 The 6TMS Ni2+ uptake transporter (HupE-UreJ) Family 2.A.100 The Ferroportin (Fpn) Family 2.A.101 The Malonate Uptake (MatC) Family (Formerly UIT1) 2.A.102 The 4-Toluene Sulfonate Uptake Permease (TSUP) Family 2.A.103 The Bacterial Murein Precursor Exporter (MPE) Family 2.A.104 The L-Alanine Exporter (AlaE) Family 2.A.105 The Mitochondrial Pyruvate Carrier (MPC) Family 2.A.106 The Ca2+:H+ Antiporter-2 (CaCA2) Family 2.A.107 The MntP Mn2+ Exporter (MntP) Family 2.A.108 The Iron/Lead Transporter (ILT) Family 2.A.109 The Tellurium Ion Resistance (TerC) Family 2.A.110 The Heme Transporter, heme-responsive gene protein (HRG) Family 2.A.111 The Na+/H+ Antiporter-E (NhaE) Family 2.A.112 The KX Blood-group Antigen (KXA) Family 2.A.113 The Nickel/cobalt Transporter (NicO) Family 2.A.114 The Putative Peptide Transporter Carbon Starvation CstA (CstA) Family 2.A.115 The Novobiocin Exporter (NbcE) Family 2.A.116 The Peptidoglycolipid Addressing Protein (GAP) Family 2.A.117 The Chlorhexadine Exporter (CHX) family 2.A.118 The Basic Amino Acid Antiporter (ArcD) Family 2.A.119 The Organo-Arsenical Exporter (ArsP) Family 2.A.120 The Putative Amino Acid Permease (PAAP) Family 2.A.121 The Sulfate Transporter (CysZ) Family 2.A.122 The LrgB/CidB holin-like auxiliary protein (LrgB/CidB) Family 2.A.123 The Sweet; PQ-loop; Saliva; MtN3 (Sweet) Family 2.A.124 The Lysine Exporter (LysO) Family 2.A.125 The Eukaryotic Riboflavin Transporter (E-RFT) Family 2.A.126 The Fatty Acid Exporter (FAX) Family 2.A.127 Enterobacterial Cardiolipin Transporter (CLT) Family
Sources: en.wikipedia.org
Peptide amphiphiles (PAs) are peptide-based molecules that self-assemble into supramolecular nanostructures including; spherical micelles, twisted ribbons, and high-aspect-ratio nanofibers. A peptide amphiphile typically comprises a hydrophilic peptide sequence attached to a lipid tail, i.e. a hydrophobic alkyl chain with 10 to 16 carbons. Therefore, they can be considered a type of lipopeptide. A special type of PA, is constituted by alternating charged and neutral residues, in a repeated pattern, such as RADA16-I. The PAs were developed in the 1990s and the early 2000s and could be used in various medical areas including: nanocarriers, nanodrugs, and imaging agents. However, perhaps their main potential is in regenerative medicine to culture and deliver cells and growth factors.
18q deletion syndrome Acrodermatitis enteropathica Acrogeria (Gottron syndrome) Acrokeratosis verruciformis (acrokeratosis verruciformis of Hopf) Adams–Oliver syndrome Adducted thumbs syndrome Albright's hereditary osteodystrophy Angelman syndrome Apert syndrome (acrocephalosyndactyly) Arthrogryposis–renal dysfunction–cholestasis syndrome Ataxia telangiectasia (Louis–Bar syndrome) Atrichia with papular lesions (papular atrichia) Atrophodermia vermiculata (acne vermoulante, acne vermoulanti, atrophoderma reticulata symmetrica faciei, atrophoderma reticulatum, atrophoderma vermiculata, atrophoderma vermiculatum, atrophodermia reticulata symmetrica faciei, atrophodermia ulerythematosa, atrophodermie vermiculée des joues avec kératoses folliculaires, folliculitis ulerythema reticulata, folliculitis ulerythematous reticulata, folliculitis ulerythemosa, honeycomb atrophy, ulerythema acneforme, ulerythema acneiforme) Autoimmune polyendocrinopathy–candidiasis–ectodermal dystrophy syndrome Bart syndrome Bazex–Dupré–Christol syndrome (Bazex syndrome, follicular atrophoderma and basal cell carcinomas) Beare–Stevenson cutis gyrata syndrome Bloom syndrome (Bloom–Torre–Machacek syndrome) Blue rubber bleb nevus syndrome Brittle hair–intellectual impairment–decreased fertility–short stature syndrome Cantú syndrome Cardio-facio-cutaneous syndrome (cardiofaciocutaneous syndrome) Cartilage–hair hypoplasia (McKusick type metaphyseal chondrodysplasia) Cerebral dysgenesis–neuropathy–ichthyosis–keratoderma syndrome Childhood tumor syndrome Chondrodysplasia punctata Cicatricial junctional epidermolysis bullosa Craniosynostosis–anal anomalies–porokeratosis syndrome Cockayne syndrome Colobomas of the eye–heart defects–ichthyosiform dermatosis–mental retardation–ear defects syndrome (CHIME syndrome, Zunich neuroectodermal syndrome, Zunich–Kaye syndrome) Congenital hemidysplasia with ichthyosiform erythroderma and limb defects syndrome (CHILD syndrome) Conradi–Hünermann syndrome (Conradi–Hünermann–Happle syndrome, Happle syndrome, X-linked dominant chondrodysplasia punctata) Costello syndrome Cronkhite–Canada syndrome Crouzon syndrome Cutis verticis gyrata Darier's disease (Darier–White disease, dyskeratosis follicularis, keratosis follicularis) DeSanctis–Cacchione syndrome Disseminated superficial actinic porokeratosis Disseminated superficial porokeratosis Dolichol kinase deficiency Dominant dystrophic epidermolysis bullosa Dyskeratosis congenita (Zinsser–Cole–Engman syndrome) Dystrophic epidermolysis bullosa Ectodermal dysplasia Ectodermal dysplasia with corkscrew hairs Ectrodactyly–ectodermal dysplasia–cleft syndrome (EEC syndrome, split hand–split foot–ectodermal dysplasia–cleft syndrome) Epidermolysis bullosa herpetiformis (Dowling–Meara epidermolysis bullosa simplex) Epidermolysis bullosa simplex Epidermolysis bullosa simplex of Ogna Epidermolysis bullosa simplex with mottled pigmentation Epidermolysis bullosa simplex with muscular dystrophy Epidermolytic hyperkeratosis (bullous congenital ichthyosiform erythroderma, bullous ichthyosiform erythroderma) Erythrokeratodermia with ataxia (Giroux–Barbeau syndrome) Familial benign chronic pemphigus (familial benign pemphigus, Hailey–Hailey disease) Fanconi syndrome (familial pancytopenia, familial panmyelophthisis) Fibrodysplasia ossificans progressiva Focal dermal hypoplasia (Goltz syndrome) Follicular atrophoderma Franceschetti–Klein syndrome (mandibulofacial dysostosis) Gardner's syndrome (familial colorectal polyposis) Gastrocutaneous syndrome Generalized atrophic benign epidermolysis bullosa Generalized epidermolysis bullosa simplex (Koebner variant of generalized epidermolysis bullosa simplex) Generalized trichoepithelioma Giant axonal neuropathy with curly hair Gingival fibromatosis with hypertrichosis Haber syndrome Hallerman–Streiff syndrome Harlequin-type ichthyosis (harlequin baby, harlequin fetus, harlequin ichthyosis, ichthyosis congenita, ichthyosis congenita gravior) Hay–Wells syndrome (AEC syndrome, ankyloblepharon filiforme adnatum–ectodermal dysplasia–cleft palate syndrome, ankyloblepharon–ectodermal defects–cleft lip and palate syndrome, ankyloblepharon–ectodermal dysplasia–clefting syndrome) Hereditary sclerosing poikiloderma Heterochromia iridum Holocarboxylase synthetase deficiency Hypohidrotic ectodermal dysplasia (anhidrotic ectodermal dysplasia, Christ–Siemens–Touraine syndrome) Hypotrichosis–acro-osteolysis–onychogryphosis–palmoplantar keratoderma–periodontitis syndrome Hypotrichosis–lymphedema–telangiectasia syndrome Ichthyosis–brittle hair–impaired intelligence–decreased fertility–short stature syndrome (IBIDS syndrome, sulfur-deficient brittle hair syndrome, Tay's syndrome, trichothiodystrophy, trichothiodystrophy with ichthyosis) Ichthyosis bullosa of Siemens (ichthyosis exfoliativa) Ichthyosis follicularis (ichthyosis follicularis with alopecia and photophobia syndrome) Ichthyosis linearis circumflexa Ichthyosis prematurity syndrome Ichthyosis vulgaris (autosomal dominant ichthyosis, ichthyosis simplex) Ichthyosis with confetti Neonatal ichthyosis–sclerosing cholangitis syndrome (ichthyosis–sclerosing cholangitis syndrome, NISCH syndrome) Incontinentia pigmenti achromians (hypomelanosis of Ito) Immune dysfunction–polyendocrinopathy–enteropathy–X-linked syndrome Jaffe–Campanacci syndrome Johanson–Blizzard syndrome Johnson–McMillin syndrome Joubert syndrome Junctional epidermolysis bullosa Junctional epidermolysis bullosa gravis (epidermolysis bullosa letalis, Herlitz disease, Herlitz epidermolysis bullosa, Herlitz syndrome, lethal junctional epidermolysis bullosa) Junctional epidermolysis bullosa with pyloric atresia Kabuki syndrome (Kabuki makeup syndrome, Niikawa–Kuroki syndrome) Keratolytic winter erythema (erythrokeratolysis hiemalis, Oudtshoorn disease, Oudtshoorn skin) Keratosis follicularis spinulosa decalvans (Siemens-1 syndrome) Keratosis linearis with ichthyosis congenita and sclerosing keratoderma syndrome Keratosis pilaris atrophicans faciei (folliculitis rubra, keratosis pilaris rubra atrophicans faciei, lichen pilare, lichen pilaire ou xerodermie pilaire symmetrique de la face, ulerythema ophryogenes, xerodermi pilaire symmetrique de la face) Keratosis pilaris Kindler syndrome (acrokeratotic poikiloderma, bullous acrokeratotic poikiloderma of Kindler and Weary, congenital poikiloderma with blisters and keratoses, congenital poikiloderma with bullae and progressive cutaneous atrophy, hereditary acrokeratotic poikiloderma, hyperkeratosis–hyperpigmentation syndrome, Weary–Kindler syndrome) Klinefelter syndrome Klippel–Feil syndrome Lamellar ichthyosis (collodion baby) Legius syndrome (neurofibromatosis type 1-like syndrome) Lelis syndrome Lenz–Majewski syndrome Leschke syndrome Lethal acantholytic epidermolysis bullosa Lhermitte–Duclos disease Linear and whorled nevoid hypermelanosis (linear nevoid hyperpigmentation, progressive cribriform and zosteriform hyperpigmentation, reticulate and zosteriform hyperpigmentation, reticulate hyperpigmentation of Iijima and Naito and Uyeno, zebra-like hyperpigmentation in whorls and streaks, zebra-line hyperpigmentation) Linear Darier disease (acantholytic dyskeratotic epidermal nevus) Linear porokeratosis Localized epidermolysis bullosa simplex (Weber–Cockayne syndrome, Weber–Cockayne variant of generalized epidermolysis bullosa simplex) Mandibuloacral dysplasia Marinesco–Sjögren syndrome McCune–Albright syndrome McCusick syndrome Metageria Microphthalmia–dermal aplasia–sclerocornea syndrome Mitis junctional epidermolysis bullosa (nonlethal junctional epidermolysis bullosa) Mitochondrial myopathy–encephalopathy–lactic acidosis–stroke syndrome Multiple lentigines syndrome (cardiocutaneous syndrome, Gorlin syndrome II, lentiginosis profusa syndrome, LEOPARD syndrome, progressive cardiomyopathic lentiginosis) Multiple pterygium syndrome Multiple sulfatase deficiency (Austin disease, mucosulfatidosis) Naegeli–Franceschetti–Jadassohn syndrome (chromatophore nevus of Naegeli) Netherton syndrome Neurofibromatosis type 1 (von Recklinghausen's disease) Neurofibromatosis type 3 (neurofibromatosis mixed type) Neurofibromatosis type 4 (neurofibromatosis variant type) Neutral lipid storage disease (Dorfman–Chanarin syndrome) Nonbullous congenital ichthyosiform erythroderma (congenital ichthyosiform erythroderma) Noonan syndrome Oculocerebrocutaneous syndrome (Delleman–Oorthuys syndrome) Oculodentodigital dysplasia Odonto-tricho-ungual-digital-palmar syndrome Oliver–McFarlane syndrome Orofaciodigital syndrome Pachydermoperiostosis (idiopathic hypertrophic osteoathorpathy, Touraine–Solente–Gole syndrome) Peeling skin syndrome (acral peeling skin syndrome, continual peeling skin syndrome, familial continual skin peeling, idiopathic deciduous skin, keratolysis exfoliativa congenita) Pfeiffer syndrome Photosensitivity–ichthyosis–brittle sulfur-deficient hair–impaired intelligence–decreased fertility–short stature syndrome Pityriasis rotunda (pityriasis circinata, tinea circinata) Plate-like osteoma cutis Plaque-type porokeratosis (classic porokeratosis, porokeratosis of Mibelli) Polyneuropathy–organomegaly–endocrinopathy–monoclonal gammopathy–skin changes syndrome (Crow–Fukase syndrome) Polyostotic fibrous dysplasia (Albright's disease) Popliteal pterygium syndrome Porokeratosis Porokeratosis palmaris et plantaris disseminata Prader–Willi syndrome Progeria (Hutchinson–Gilford progeria syndrome, Hutchinson–Gilford syndrome, progeria syndrome) Progressive osseous heteroplasia Progressive symmetric erythrokeratodermia (erythrokeratodermia progressiva symmetrica) Proteus syndrome Proteus-like syndrome Punctate porokeratosis Rapp–Hodgkin syndrome (Rapp–Hodgkin ectodermal dysplasia syndrome) Recessive dystrophic epidermolysis bullosa (Hallopeau–Siemens variant of epidermolysis bullosa, Hallopeau–Siemens disease) Refsum's disease (heredopathia atactica polyneuritiformis, phytanic acid storage disease) Relapsing linear acantholytic dermatosis Restrictive dermopathy Rhizomelic chondrodysplasia punctata (autosomal recessive chondrodysplasia punctata type 1, chondrodystrophia calcificans punctata, peroxisomal biogenesis disorder complementation group 11) Rombo syndrome Rothmund–Thomson syndrome (poikiloderma congenitale) Rud syndrome Say syndrome Scalp–ear–nipple syndrome (Finlay–Marks syndrome) Schindler disease (Kanzaki disease, alpha-N-acetylgalactosaminidase deficiency) Schinzel–Giedion syndrome Scleroatrophic syndrome of Huriez (Huriez syndrome, palmoplantar keratoderma with scleroatrophy, palmoplantar keratoderma with sclerodactyly, scleroatrophic and keratotic dermatosis of the limbs, sclerotylosis) Segmental neurofibromatosis Senter syndrome (Desmons' syndrome) Shabbir syndrome (laryngo–onycho–cutaneous syndrome) Silver–Russell syndrome Sjögren–Larsson syndrome Skin fragility syndrome (plakophilin 1 deficiency) Smith–Lemli–Opitz syndrome Sturge–Weber syndrome Supernumerary nipples–uropathies–Becker's nevus syndrome Terminal osseous dysplasia with pigmentary defects Tooth and nail syndrome (hypodontia with nail dysgenesis, Witkop syndrome) Townes–Brocks syndrome Transient bullous dermolysis of the newborn Treacher Collins syndrome (Treacher Collins–Franceschetti syndrome) Tricho–dento–osseous syndrome Tricho–rhino–phalangeal syndrome Tuberous sclerosis (Bourneville disease, epiloia) Turner syndrome Ulnar–mammary syndrome Van Der Woude syndrome Von Hippel–Lindau syndrome Watson syndrome Werner syndrome (adult progeria) Westerhof syndrome Whistling syndrome (craniocarpotarsal syndrome, distal arthrogryposis type 2, Freeman–Sheldon syndrome, Windmill–Vane–Hand syndrome) Wilson–Turner syndrome Wolf–Hirschhorn syndrome (4p- syndrome) X-linked ichthyosis (steroid sulfatase deficiency, X-linked recessive ichthyosis) X-linked recessive chondrodysplasia punctata Xeroderma pigmentosum (Cockayne syndrome complex) XXYY genotype Zimmermann–Laband syndrome
Brinkley initiated a boom in male impotence treatments in the U.S. in the 1920s and 1930s, with radio programs that recommended expensive goat gland implants and "mercurochrome" injections as the path to restored male virility, including operations by surgeon Serge Voronoff. Modern drug therapy for ED made a significant advance in 1983, when British physiologist Giles Brindley dropped his trousers and demonstrated to a shocked Urodynamics Society audience showing his papaverine-induced erection. The current most common treatment for ED, the oral PDE5 inhibitor known as sildenafil (Viagra) was approved for use for Pfizer by the FDA in 1998, which at the time of release was the fastest selling drug in history. Sildenafil largely replaced SSRI treatments for ED at the time and proliferated new types of specialised pharmaceutical marketing which emphasised social connotations of ED and Viagra rather than its physical effects.
Everyone, Wherever You Are, Come One Step Closer: Questions about God. Translated by Tony Crawford. Cambridge, UK: Polity Press. ISBN 978-1-5095-5628-1. OCLC 1389811523. Kermani, Navid (2023). What Is Possible Now: 33 Political Situations. Translated by Tony Crawford. Cambridge, UK: Polity Press. ISBN 978-1-5095-5764-6. OCLC 1378713376. Kermani, Navid (2026): In the Other Direction Now. Dispatches from East Africa. Haus Publishing, London 2026, ISBN 978-1-914982-22-4. Translated by Tony Crawford; In die andere Richtung jetzt. Eine Reise durch Ostafrika. C.H. Beck, München 2024, ISBN 978-3-406-81969-8; Rezension von Wolfram Schütte.
Sources: en.wikipedia.org
These findings suggest specific parasite loci may be under vaccine-induced immune pressure and highlight potential targets for future optimization of whole-sporozoite vaccines. PfSPZ Vaccine development has been closely linked with malaria elimination efforts on Bioko Island, Equatorial Guinea. By 2024–2025, a series of registry studies, incidence surveys and dose-optimization trials had been completed as part of preparations for a large-scale, Africa-led phase 3 efficacy trial. These activities were coordinated through the Equatoguinean Malaria Vaccine Initiative, which aims to evaluate PfSPZ Vaccine in a setting with intense seasonal transmission and established malaria control programs.
=== Lithuania === Lithuanian Armed Forces field rations are based on the American MRE. They come in 10 menus packed in a dark green plastic bag, and besides the main meal in a retort pouch they also include two small dark chocolate bars, honey or jam, four hard-tack biscuits, a handful of almonds or hazelnuts, instant drink mix, tea or coffee, sugar, an antiseptic wipe, matches, solid fuel tablets, a flat disposable stove, a flameless heater (similar to the US one) and a cable-tie used to seal waste packaging back into the outer bag after use.
{\displaystyle T\leq {\frac {abc}{2}}{\sqrt {\frac {a+b+c}{a^{3}+b^{3}+c^{3}+abc}}}\leq {\frac {1}{4}}{\sqrt[{6}]{\frac {3(a+b+c)^{3}(abc)^{4}}{a^{3}+b^{3}+c^{3}}}}\leq {\frac {\sqrt {3}}{4}}(abc)^{\frac {2}{3}}.}
Sources: en.wikipedia.org
Most published work uses intranasal application, either as drops or as a nasal spray. Injection routes appear in a smaller set of animal experiments. Oral use is uncommon in the literature because peptide breakdown and poor absorption limit this route.
Reported human trials are few, brief and originate mainly from one country. They describe effects on anxiety-related measures, but sample sizes are small and reporting is limited. The results are widely regarded as preliminary rather than confirmed.
Reverse-phase liquid chromatography is used to assess purity and separation of related impurities. Mass spectrometry confirms that the observed molecular mass matches the expected peptide. A certificate of analysis from the supplier is the usual document of record.
Selank is a synthetic peptide made of seven amino acids. It is modeled on tuftsin, a natural tetrapeptide, with an added three-residue tail. It is not a small-molecule drug.