Cas no 80451-05-4 (Cecropin B)

Cecropin B is a cationic antimicrobial peptide (AMP) originally isolated from the giant silk moth Hyalophora cecropia. It exhibits broad-spectrum activity against Gram-negative and Gram-positive bacteria, fungi, and certain parasites. The peptide disrupts microbial membranes through electrostatic interactions with negatively charged phospholipids, leading to cell lysis. Its mechanism of action reduces the likelihood of resistance development compared to conventional antibiotics. Cecropin B is also stable under physiological conditions and demonstrates low cytotoxicity toward mammalian cells, making it a promising candidate for therapeutic and biomedical applications. Research continues to explore its potential in antimicrobial coatings, drug delivery, and immunomodulation.
Cecropin B structure
Cecropin B structure
Product Name:Cecropin B
CAS No:80451-05-4
MF:C176H302N52O41S
MW:3834.66991758347
MDL:MFCD00130753
CID:721720
PubChem ID:16130488
Update Time:2025-06-13

Cecropin B Chemical and Physical Properties

Names and Identifiers

    • Cecropin B (Platysamiacecropia antibacterial peptide) (9CI)
    • Cecropin B
    • LYS-TRP-LYS-VAL-PHE-LYS-LYS-ILE-GLU-LYS-MET-GLY-ARG-ASN-ILE-ARG-ASN-GLY-ILE-VAL-LYS-ALA-GLY-PRO-ALA-ILE-ALA-VAL-LEU-GLY-GLU-ALA-LYS-ALA-LEU-NH2
    • Cecropin B protein, Hyalophora cecropia
    • DTXSID90230334
    • P9B protein, Hyalophora cecropia
    • P9B protein, Insecta
    • Cecropin B protein,Insecta
    • P9B Protein
    • EX-A7391
    • cecropin B protein, Insecta
    • CHEMBL1673088
    • 80451-05-4
    • DTXCID90152825
    • DA-62171
    • MDL： MFCD00130753
    • Inchi： 1S/C176H302N52O41S/c1-25-97(15)140(174(269)224-139(96(13)14)168(263)212-113(57-36-43-72-179)155(250)199-101(19)145(240)198-91-134(234)228-79-50-64-128(228)167(262)202-104(22)149(244)225-141(98(16)26-2)171(266)203-105(23)148(243)222-137(94(9)10)169(264)219-123(82-93(7)8)152(247)196-89-132(232)205-119(65-67-135(235)236)156(251)201-102(20)146(241)206-112(56-35-42-71-178)154(249)200-103(21)147(242)215-122(144(187)239)81-92(5)6)221-133(233)90-197-153(248)126(85-129(185)229)217-160(255)118(63-49-78-193-176(190)191)213-172(267)143(100(18)28-4)227-166(261)127(86-130(186)230)218-157(252)111(62-48-77-192-175(188)189)204-131(231)88-195-151(246)121(69-80-270-24)211-159(254)114(58-37-44-73-180)207-161(256)120(66-68-136(237)238)214-173(268)142(99(17)27-3)226-163(258)117(61-40-47-76-183)208-158(253)115(59-38-45-74-181)209-164(259)124(83-106-51-30-29-31-52-106)220-170(265)138(95(11)12)223-162(257)116(60-39-46-75-182)210-165(260)125(216-150(245)109(184)54-34-41-70-177)84-107-87-194-110-55-33-32-53-108(107)110/h29-33,51-53,55,87,92-105,109,111-128,137-143,194H,25-28,34-50,54,56-86,88-91,177-184H2,1-24H3,(H2,185,229)(H2,186,230)(H2,187,239)(H,195,246)(H,196,247)(H,197,248)(H,198,240)(H,199,250)(H,200,249)(H,201,251)(H,202,262)(H,203,266)(H,204,231)(H,205,232)(H,206,241)(H,207,256)(H,208,253)(H,209,259)(H,210,260)(H,211,254)(H,212,263)(H,213,267)(H,214,268)(H,215,242)(H,216,245)(H,217,255)(H,218,252)(H,219,264)(H,220,265)(H,221,233)(H,222,243)(H,223,257)(H,224,269)(H,225,244)(H,226,258)(H,227,261)(H,235,236)(H,237,238)(H4,188,189,192)(H4,190,191,193)/t97-,98-,99-,100-,101-,102-,103-,104-,105-,109-,111-,112-,113-,114-,115-,116-,117-,118-,119-,120-,121-,122-,123-,124-,125-,126-,127-,128-,137-,138-,139-,140-,141-,142-,143-/m0/s1
    • InChI Key： YIQHNFUJWYYSEC-MQAAYMCRSA-N
    • SMILES： S(C)CC[C@@H](C(NCC(N[C@@H](CCCNC(=N)N)C(N[C@@H](CC(N)=O)C(N[C@H](C(N[C@H](C(N[C@@H](CC(N)=O)C(NCC(N[C@H](C(N[C@@H](C(C)C)C(N[C@@H](CCCCN)C(N[C@@H](C)C(NCC(N1CCC[C@H]1C(N[C@@H](C)C(N[C@H](C(N[C@@H](C)C(N[C@H](C(N[C@H](C(NCC(N[C@H](C(N[C@@H](C)C(N[C@H](C(N[C@@H](C)C(N[C@H](C(N)=O)CC(C)C)=O)=O)CCCCN)=O)=O)CCC(=O)O)=O)=O)CC(C)C)=O)C(C)C)=O)=O)[C@@H](C)CC)=O)=O)=O)=O)=O)=O)=O)[C@@H](C)CC)=O)=O)=O)CCCNC(=N)N)=O)[C@@H](C)CC)=O)=O)=O)=O)NC([C@H](CCCCN)NC([C@H](CCC(=O)O)NC([C@H]([C@@H](C)CC)NC([C@H](CCCCN)NC([C@H](CCCCN)NC([C@H](CC1C=CC=CC=1)NC([C@H](C(C)C)NC([C@H](CCCCN)NC([C@H](CC1=CNC2C=CC=CC1=2)NC([C@H](CCCCN)N)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O

Computed Properties

  • Exact Mass: 3833.289933
  • Monoisotopic Mass: 3832.286578
  • Isotope Atom Count: 0
  • Hydrogen Bond Donor Count: 53
  • Hydrogen Bond Acceptor Count: 52
  • Heavy Atom Count: 270
  • Rotatable Bond Count: 138
  • Complexity: 8830
  • Covalently-Bonded Unit Count: 1
  • Defined Atom Stereocenter Count: 35
  • Undefined Atom Stereocenter Count : 0
  • Defined Bond Stereocenter Count: 0
  • Undefined Bond Stereocenter Count: 0
  • Topological Polar Surface Area: 1560
  • XLogP3: -8.4

Cecropin B Security Information

  • Hazardous Material transportation number：NONH for all modes of transport
  • WGK Germany：3
  • Storage Condition：Powder -80°C 2 years ? -20°C 1 year In solvent -80°C 6 months ? -20°C 1 month

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Cecropin B Related Literature

Related Categories

Additional information on Cecropin B

Exploring Cecropin B (CAS No. 80451-05-4): A Potent Antimicrobial Peptide with Therapeutic Potential

Cecropin B (CAS No. 80451-05-4) is a naturally occurring antimicrobial peptide (AMP) first isolated from the hemolymph of the giant silk moth, Hyalophora cecropia. This cationic peptide belongs to the cecropin family, renowned for its broad-spectrum activity against bacteria, fungi, and even some enveloped viruses. With the rise of antibiotic resistance, researchers are increasingly focusing on AMPs like Cecropin B as potential alternatives to conventional antibiotics.

The molecular structure of Cecropin B features an amphipathic α-helix, enabling it to disrupt microbial membranes selectively. Unlike traditional antibiotics, which target specific metabolic pathways, Cecropin B physically perforates cell membranes, making it harder for pathogens to develop resistance. This mechanism has sparked interest in its applications for wound healing, food preservation, and even cancer therapy due to its selective toxicity toward malignant cells.

Recent studies highlight Cecropin B's synergy with existing drugs. For instance, combined with colistin, it shows enhanced efficacy against multidrug-resistant Gram-negative bacteria, a pressing concern in hospitals worldwide. Users searching for "peptide-based antibiotics" or "natural antimicrobial agents" will find Cecropin B a compelling subject, especially amid the global push for One Health strategies to combat superbugs.

From a biotechnological perspective, Cecropin B (CAS No. 80451-05-4) is produced via recombinant DNA technology or solid-phase peptide synthesis. Its stability can be optimized through D-amino acid substitutions or PEGylation, addressing common challenges like proteolytic degradation—a hot topic in "peptide drug delivery" research. Startups exploring "bioengineered antimicrobials" often cite Cecropin B as a model compound.

Beyond medicine, Cecropin B has agricultural applications. Farmers searching for "alternatives to livestock antibiotics" may encounter studies where Cecropin B-infused feed reduces Salmonella colonization in poultry. Similarly, its use in biodegradable food packaging aligns with trends toward "green preservatives," appealing to eco-conscious consumers.

Despite its promise, challenges remain. Cecropin B's hemolytic activity at high concentrations necessitates careful dosage control. Researchers investigating "peptide toxicity reduction" are exploring truncated analogs or hybrid peptides to mitigate side effects. Meanwhile, advances in nanocarrier systems could enhance its targeted delivery, a frequent query in "nanomedicine forums."

In conclusion, Cecropin B (CAS No. 80451-05-4) exemplifies the potential of host defense peptides in addressing modern health crises. Its multifaceted applications—from combating antibiotic-resistant infections to enabling sustainable agriculture—make it a focal point for interdisciplinary research. As interest grows in "next-gen antimicrobials," this peptide continues to inspire innovations at the nexus of biology, chemistry, and engineering.

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