Staphylococcus epidermidis has emerged as the main causative agent for graft-related and nosocomial infections. Rampant use of antibiotics and biofilm formed by the organism results in poor penetration of the drug and further aggravates the antibiotic resistance, emphasizing an urgent need to explore alternative treatment modalities. Antimicrobial peptides (AMPs), produced as effector molecules of the innate immunity of living organisms, have therapeutic potential that can be used to inhibit the growth of microbes. In addition, the susceptibility of a microbe to become resistant to an AMP is relatively low. The AMPs are amphipathic peptides of 12-100 residues, which have broad-spectrum activity against microbes. There are scattered reports of AMPs listed against S. epidermidis and there is an urgent need to systematically study the AMPs. Various natural AMPs as well as synthetic peptides have been investigated against S. epidermidis. These peptides have been shown to inhibit both planktonic culture and S. epidermidis biofilm effectively. The multiple modes of action in killing the organism minimize the chances for the development of resistance. This review focused on various natural and synthetic peptides that demonstrate activity against S. epidermidis.
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http://dx.doi.org/10.1159/000443479 | DOI Listing |
Adv Sci (Weinh)
January 2025
Department of Biological Sciences and Biotechnology, College of Natural Sciences, Chungbuk National University, Cheongju, Chungbuk, 28644, Republic of Korea.
Antimicrobial peptides (AMPs) are promising agents for treating antibiotic-resistant bacterial infections. Although discovering novel AMPs is crucial for combating multidrug-resistant bacteria and biofilm-related infections, their clinical potential relies on precise, real-time evaluation of efficacy, toxicity, and mechanisms. Optical diffraction tomography (ODT), a label-free imaging technology, enables real-time visualization of bacterial morphological changes, membrane damage, and biofilm formation over time.
View Article and Find Full Text PDFJ Chem Inf Model
January 2025
School of Information and Artificial Intelligence, Anhui Provincial Engineering Research Center for Beidou Precision Agriculture Information, Key Laboratory of Agricultural Sensors for Ministry of Agriculture and Rural Affairs, Anhui Agricultural University, Hefei, Anhui 230036, China.
Antimicrobial peptides (AMPs) are small peptides that play an important role in disease defense. As the problem of pathogen resistance caused by the misuse of antibiotics intensifies, the identification of AMPs as alternatives to antibiotics has become a hot topic. Accurately identifying AMPs using computational methods has been a key issue in the field of bioinformatics in recent years.
View Article and Find Full Text PDFACS Appl Bio Mater
January 2025
School of Chemistry, Pharmacy and Food Biosciences, University of Reading, Whiteknights, Reading RG6 6AD, U.K.
A series of tripodal (three-arm) lysine-based peptides were designed and synthesized and their self-assembly properties in aqueous solution and antimicrobial activity were investigated. We compare the behaviors of homochiral tripodal peptides (KKY)K and a homologue containing the bulky aromatic fluorenylmethoxycarbonyl (Fmoc) group Fmoc-(KKY)K, and heterochiral analogues containing k (d-Lys), (kkY)K and Fmoc-(kkY)K. The molecular conformation and self-assembly in aqueous solutions were probed using various spectroscopic techniques, along with small-angle X-ray scattering (SAXS) and cryogenic-transmission electron microscopy (cryo-TEM).
View Article and Find Full Text PDFProtein Pept Lett
January 2025
Department of Biology, Faculty of Science, Ege University, Izmir, Turkey.
Like other vertebrates, amphibians possess innate and adaptive immune systems. At the center of the adaptive immune system is the Major Histocompatibility Complex. The important molecules of innate immunity are antimicrobial peptides (AMPs).
View Article and Find Full Text PDFBiochim Biophys Acta Biomembr
January 2025
Biochemistry and Molecular Biology Department, Center for Pharmaceutical Research and Development, Ave. 26 # 1605, Nuevo Vedado, Ciudad de La Habana, 10400, Cuba. Electronic address:
Acylation is a common method used to modify antimicrobial peptides to enhance their effectiveness. It increases the interactions between the peptide and the bacterial cell membranes. However, acylation can also reduce the selectivity of the peptides by making them more active on eukaryotic membranes, which can lead to unintended toxicity.
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