1001644-68-3
Chemical Structure
Antimicrobial peptide BP100
- CAS No.: 1001644-68-3
- Formula:C72H125N17O12
- Molecular Weight:1420.87
InChIKey: QIQRVOMSZCHJLT-AQKDKPMWSA-N
SMILES: OC(C=C1)=CC=C1C[C@@H](C(N[C@H](C(N)=O)CC(C)C)=O)NC([C@H](CCCCN)NC([C@H](CC(C)C)NC([C@H]([C@@H](C)CC)NC([C@H](CCCCN)NC([C@H](CCCCN)NC([C@@H](NC([C@H](CC(C)C)NC([C@H](CCCCN)NC([C@@H](N)CCCCN)=O)=O)=O)CC2=CC=CC=C2)=O)=O)=O)=O)=O)=O
Biological Activity: Antimicrobial peptide BP100 is a linear undecapeptide with an amphipathic α-helical structure that exhibits antibacterial activity. Antimicrobial peptide BP100 shows in vitro antibacterial activity against a variety of plant and human pathogens. Antimicrobial peptide BP100 binds to and inserts into bacterial cell membranes through electrostatic attraction, triggering membrane permeabilization and ultimately leading to membrane disruption. Antimicrobial peptide BP100 can be used for research on bacterial infections[1][2][3][4][5].
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Antimicrobial peptide BP100 | Antimicrobial peptide BP100 is a linear undecapeptide with an amphipathic α-helical structure that exhibits antibacterial activity. Antimicrobial peptide BP100 shows in vitro antibacterial activity against a variety of plant and human pathogens. Antimicrobial peptide BP100 binds to and inserts into bacterial cell membranes through electrostatic attraction, triggering membrane permeabilization and ultimately leading to membrane disruption. Antimicrobial peptide BP100 can be used for research on bacterial infections. | |||||||||||||||||||||
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References
- [1]. Riesco-Llach G, et al. Deciphering the Mechanism of Action of the Antimicrobial Peptide BP100. International journal of molecular sciences. 2024 Mar 19;25(6):3456.
- [2]. Oddo A, et al. An Amphipathic Undecapeptide with All d-Amino Acids Shows Promising Activity against Colistin-Resistant Strains of Acinetobacter baumannii and a Dual Mode of Action. Antimicrobial agents and chemotherapy. 2016 Jan;60(1):592-9.
- [3]. Oliveras À, et al. Peptide Conjugates Derived from flg15, Pep13, and PIP1 That Are Active against Plant-Pathogenic Bacteria and Trigger Plant Defense Responses. Applied and environmental microbiology. 2022 Jun 28;88(12):e0057422.
- [4]. Alves CS, et al. Escherichia coli cell surface perturbation and disruption induced by antimicrobial peptides BP100 and pepR. The Journal of biological chemistry. 2010 Sep 03;285(36):27536-44.
- [5]. Nadal A, et al. Constitutive expression of transgenes encoding derivatives of the synthetic antimicrobial peptide BP100: impact on rice host plant fitness. BMC plant biology. 2012 Sep 04;12:159.
