HNP-1, a-Defensin-1, Human Neutrophil Peptide-1

Product Name: HNP-1, a-Defensin-1, Human Neutrophil Peptide-1

Sequence One Letter Code: ACYCRIPACIAGERRYGTCIYQGRLWAFCC (Disulfide bridge: 2-30, 4-19, 9-29)

Sequence Three Letter Code: H-Ala-Cys-Tyr-Cys-Arg-Ile-Pro-Ala-Cys-Ile-Ala-Gly-Glu-Arg-Arg-Tyr-Gly-Thr-Cys-Ile-Tyr-Gln-Gly-Arg-Leu-Trp-Ala-Phe-Cys-Cys-OH (Disulfide bridge: 2-30, 4-19, 9-29)

Cas No: 136661-76-2

Chemical Formula:C150H222N44O38S6

Molecular Weight: 3442.1

Purity: 95%

Form: Lyophilized

Storage Conditions: - 20 °C

Research Area: Infection Disease Research

SMILES: CC[C@H](C)[C@H]1C(=O)N[C@H](C(=O)NCC(=O)N[C@H](C(=O)N[C@H](C(=O)N[C@H](C(=O)N[C@H](C(=O)NCC(=O)N[C@H](C(=O)N[C@H]2CSSC[C@H]3C(=O)N[C@H](C(=O)N[C@H](C(=O)N4CCC[C@H]4C(=O)N[C@H](C(=O)N[C@@H](CSSC[C@@H](C(=O)N[C@@H](CSSC[C@@H](C(=O)N[C@H](C(=O)N3)CC5=CC=C(C=C5)O)NC(=O)[C@H](C)N)C(=O)O)NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)CNC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@@H](NC2=O)[C@@H](C)CC)CC6=CC=C(C=C6)O)CCC(=O)N)CCCNC(=N)N)CC(C)C)CC7=CNC8=CC=CC=C87)C)CC9=CC=CC=C9)C(=O)N1)C)[C@@H](C)CC)CCCNC(=N)N)[C@@H](C)O)CC1=CC=C(C=C1)O)CCCNC(=N)N)CCCNC(=N)N)CCC(=O)O)C

IUPAC: (1R,4S,7S,13S,16S,19R,22S,25S,31S,34S,37S,40S,46S,49R,52S,55S,58S,64S,67S,70S,73S,76S,79R,82R,87R,90S)-58-(3-amino-3-oxopropyl)-87-[[(2S)-2-aminopropanoyl]amino]-76-benzyl-7,22,52-tris[(2S)-butan-2-yl]-4,34,37,64-tetrakis(3-carbamimidamidopropyl)-31-(2-carboxyethyl)-46-[(1R)-1-hydroxyethyl]-40,55,90-tris[(4-hydroxyphenyl)methyl]-70-(1H-indol-3-ylmethyl)-16,25,73-trimethyl-67-(2-methylpropyl)-2,5,8,14,17,20,23,26,29,32,35,38,41,44,47,50,53,56,59,62,65,68,71,74,77,80,88,91-octacosaoxo-84,85,94,95,98,99-hexathia-3,6,9,15,18,21,24,27,30,33,36,39,42,45,48,51,54,57,60,63,66,69,72,75,78,81,89,92-octacosazatetracyclo[47.43.4.419,79.09,13]hectane-82-carboxylic acid

INCHIKEY: KRJOFJHOZZPBKI-KSWODRSDSA-N

INCHI:

InChI=1S/C150H222N44O38S6/c1-14-74(6)116-142(227)171-78(10)121(206)166-64-112(200)173-97(49-51-115(203)204)129(214)175-93(32-23-53-162-148(155)156)127(212)174-94(33-24-54-163-149(157)158)128(213)180-99(59-83-36-42-87(196)43-37-83)125(210)168-66-114(202)190-119(81(13)195)144(229)188-108-71-236-233-68-105-136(221)176-95(34-25-55-164-150(159)160)130(215)193-118(76(8)16-3)145(230)194-56-26-35-110(194)141(226)170-80(12)123(208)185-107(139(224)191-116)70-235-234-69-106(138(223)189-109(146(231)232)72-238-237-67-104(184-120(205)77(9)151)137(222)181-101(135(220)186-105)60-84-38-44-88(197)45-39-84)187-134(219)100(58-82-27-18-17-19-28-82)178-122(207)79(11)169-131(216)103(62-86-63-165-91-30-21-20-29-90(86)91)182-132(217)98(57-73(4)5)179-126(211)92(31-22-52-161-147(153)154)172-113(201)65-167-124(209)96(48-50-111(152)199)177-133(218)102(61-85-40-46-89(198)47-41-85)183-143(228)117(75(7)15-2)192-140(108)225/h17-21,27-30,36-47,63,73-81,92-110,116-119,165,195-198H,14-16,22-26,31-35,48-62,64-72,151H2,1-13H3,(H2,152,199)(H,166,206)(H,167,209)(H,168,210)(H,169,216)(H,170,226)(H,171,227)(H,172,201)(H,173,200)(H,174,212)(H,175,214)(H,176,221)(H,177,218)(H,178,207)(H,179,211)(H,180,213)(H,181,222)(H,182,217)(H,183,228)(H,184,205)(H,185,208)(H,186,220)(H,187,219)(H,188,229)(H,189,223)(H,190,202)(H,191,224)(H,192,225)(H,193,215)(H,203,204)(H,231,232)(H4,153,154,161)(H4,155,156,162)(H4,157,158,163)(H4,159,160,164)/t74-,75-,76-,77-,78-,79-,80-,81+,92-,93-,94-,95-,96-,97-,98-,99-,100-,101-,102-,103-,104-,105-,106-,107-,108-,109-,110-,116-,117-,118-,119-/m0/s1

Source / Species: human

Conjugation: Unconjugated

Code Nacres: NA.26

Application: HNP-1 (α-Defensin-1) is a cationic antimicrobial peptide stored in the azurophilic granules of human neutrophils. As a member of the α-defensin family, it exhibits broad-spectrum activity against Gram-positive and Gram-negative bacteria and demonstrates antiviral effects in experimental systems. HNP-1 disrupts microbial membranes and modulates immune signaling pathways. It is widely used in host–pathogen interaction research, innate immunity studies, and antimicrobial mechanism investigations. The peptide also serves as a model for analyzing defensin structure, disulfide bonding, and immune effector function.

Current Research: HNP-1 (α-Defensin-1) is a 29–amino acid cationic antimicrobial peptide belonging to the human α-defensin family. It is stored in high concentrations within the azurophilic granules of neutrophils and released rapidly upon activation during infection or inflammatory stimulation. As a key component of the innate immune response, HNP-1 provides immediate antimicrobial defense at sites of tissue injury and microbial invasion. Its broad-spectrum activity and immunomodulatory functions make it a central molecule in host–pathogen interaction research. Structural Characteristics HNP-1 contains six conserved cysteine residues that form three intramolecular disulfide bonds, creating a compact β-sheet–rich structure characteristic of α-defensins. This disulfide-stabilized conformation confers structural rigidity and resistance to proteolytic degradation. The peptide’s strong net positive charge facilitates electrostatic interactions with negatively charged microbial membranes, while its amphipathic properties enable insertion into lipid bilayers. Because of its well-defined disulfide bonding pattern, HNP-1 serves as a model system for studying defensin folding, oxidative bond formation, and structure–function relationships. Antimicrobial Mechanisms HNP-1 exerts direct microbicidal effects primarily through membrane-targeting mechanisms. Upon binding to microbial surfaces, it can disrupt membrane integrity, induce pore formation, and destabilize lipid bilayers. These actions compromise membrane permeability, leading to leakage of intracellular contents and microbial cell death. The peptide demonstrates activity against: Gram-positive bacteria Gram-negative bacteria Select fungal species Certain enveloped viruses In viral systems, HNP-1 can interfere with viral entry and replication processes, highlighting its multifunctional defensive role. Immunomodulatory Functions Beyond direct antimicrobial activity, HNP-1 modulates immune signaling pathways. It can influence cytokine production, chemotaxis, and dendritic cell activation. HNP-1 has been shown to interact with pattern recognition receptors and regulate NF-κB–dependent transcriptional responses. In addition, the peptide can act as a chemoattractant for immune cells, facilitating recruitment of monocytes and T lymphocytes to sites of infection. These properties position HNP-1 as both an effector molecule and an immunoregulatory mediator. Applications in Research HNP-1 is widely used in: Host–pathogen interaction studies Antimicrobial activity assays Membrane permeabilization experiments Cytokine induction and immune signaling analysis Viral inhibition models Structural biology investigations of defensin folding In inflammatory disease research, altered defensin expression has been associated with sepsis, chronic lung disease, and autoimmune conditions, further expanding its research relevance. Structure–Function and Peptide Engineering Because α-defensins represent prototypical cysteine-rich antimicrobial peptides, HNP-1 provides a template for peptide engineering. Mutational studies examining cysteine substitutions or charge alterations help clarify how structural features determine antimicrobial potency and immune-modulating activity. Its compact and reproducible structure supports high-resolution biophysical analyses, including NMR and crystallographic studies. Experimental Advantages Broad-spectrum antimicrobial activity Stable disulfide-bonded structure Dual antimicrobial and immunomodulatory functions Suitable for biochemical, microbiological, and cell-based assays Model scaffold for defensin engineering studies Research Significance HNP-1 (α-Defensin-1) is a central effector molecule in innate immunity and a foundational tool in infection biology research. By combining direct microbicidal activity with immune signaling modulation, it provides insight into early host defense mechanisms. Its well-characterized structure and function make it invaluable for studying antimicrobial peptide biology, immune regulation, and therapeutic development targeting infectious and inflammatory diseases.