Results 41 to 50 of about 260,388 (313)

Chain-end modifications and sequence arrangements of antimicrobial peptoids for mediating activity and nano-assembly [PDF]

, 2020
Poly(N-substituted glycine) “peptoids” are an interesting class of peptidomimics that can resist proteolysis and mimic naturally found antimicrobial peptides (AMPs), which exhibit wide spectrum activity against bacteria.
Castelletto, Valeria, Hamley, Ian W., Hasan, Abshar, Lau, King Hang Aaron, Pandey, Lalit M., Ruokolainen, Janne, Saxena, Varun, Sefcik, Jan, Seitsonen, Jani, Zimbitas, Georgina   +9 more
core   +2 more sources

Polylactic Glycolic Acid-Mediated Delivery of Plectasin Derivative NZ2114 in Staphylococcus epidermidis Biofilms

Antibiotics
Antimicrobial peptides (AMPs) are antibiotic candidates; however, their instability and protease susceptibility limit clinical applications. In this study, the polylactic acid–glycolic acid (PLGA)–polyvinyl alcohol (PVA) drug delivery system was screened
Xuanxuan Ma, Na Yang, Ruoyu Mao, Ya Hao, Da Teng, Yinhua Huang, Jianhua Wang   +6 more
doaj   +1 more source

Recent advances in the field of antimicrobial peptides in inflammatory diseases

Advanced Biomedical Research, 2013
Antimicrobial peptides are cationic molecules, which participate in multiple aspects of the immune response including the control of inflammatory diseases, characteristic that make these molecules attractive as therapeutic tools.
Patricia Méndez-Samperio
doaj   +1 more source

Antimicrobial Peptides in Reptiles

Pharmaceuticals, 2014
Reptiles are among the oldest known amniotes and are highly diverse in their morphology and ecological niches. These animals have an evolutionarily ancient innate-immune system that is of great interest to scientists trying to identify new and useful ...
Monique L. van Hoek
doaj   +1 more source

Enhanced antifouling properties of marine antimicrobial peptides by PEGylation

Frontiers in Bioengineering and Biotechnology, 2023
Covalent immobilisation of antimicrobial peptides (AMPs) on underwater surfaces to combat marine biofouling is of great interest as it is an efficient, broad-spectrum and environmentally friendly strategy.
Tong Lou, Xiuqin Bai, Xiuqin Bai, Xiaoyan He, Xiaoyan He, Wencheng Liu, Zongcheng Yang, Ying Yang, Chengqing Yuan   +8 more
doaj   +1 more source

Bioengineering Lantibiotics for Therapeutic Success [PDF]

, 2015
peer-reviewedSeveral examples of highly modified antimicrobial peptides have been described. While many such peptides are non-ribosomally synthesized, ribosomally synthesized equivalents are being discovered with increased frequency. Of the latter group,
Cotter, Paul D., Field, Des, Hill, Colin, Ross, R Paul   +3 more
core   +2 more sources

A Uniform In Vitro Efficacy Dataset to Guide Antimicrobial Peptide Design

Data, 2019
Antimicrobial peptides are ubiquitous molecules that form the innate immune system of organisms across all kingdoms of life. Despite their prevalence and early origins, they continue to remain potent natural antimicrobial agents.
Deepesh Nagarajan, Tushar Nagarajan, Neha Nanajkar, Nagasuma Chandra   +3 more
doaj   +1 more source

Self-assembly antimicrobial peptide for treatment of multidrug-resistant bacterial infection

Journal of Nanobiotechnology
The wide-spreading of multidrug resistance poses a significant threat to human and animal health. Although antimicrobial peptides (AMPs) show great potential application, their instability has severely limited their clinical application.
Xuanxuan Ma, Na Yang, Ruoyu Mao, Ya Hao, Yuanyuan Li, Ying Guo, Da Teng, Yinhua Huang, Jianhua Wang   +8 more
doaj   +1 more source

Rational Designed Hybrid Peptides Show up to a 6-Fold Increase in Antimicrobial Activity and Demonstrate Different Ultrastructural Changes as the Parental Peptides Measured by BioSAXS

Frontiers in Pharmacology, 2021
Antimicrobial peptides (AMPs) are a promising class of compounds being developed against multi-drug resistant bacteria. Hybridization has been reported to increase antimicrobial activity. Here, two proline-rich peptides (consP1: VRKPPYLPRPRPRPL-CONH2 and
Kai Hilpert, Jurnorain Gani, Christoph Rumancev, Nathan Simpson, Paula Matilde Lopez-Perez, Vasil M. Garamus, Andreas Robert von Gundlach, Petar Markov, Marco Scocchi, Ralf Mikut, Axel Rosenhahn   +10 more
doaj   +1 more source

Free energy barrier for melittin reorientation from a membrane-bound state to a transmembrane state [PDF]

, 2013
An important step in a phospholipid membrane pore formation by melittin antimicrobial peptide is a reorientation of the peptide from a surface into a transmembrane conformation.
Allende D., Almeida P. F., Andersson M., Berneche S., Chen F. Y., Constantinescu I., de Jongh H. H. J., Glattli A., Gordon-Grossman M., Hess B., Hristova K., Huang H. W., Huang H. W., Humphrey W., Irudayam S. J., Irudayam S. J., Jämbeck J. P. M., Klocek G., Kuchinka E., Ladokhin A. S., Lam K. L. H., Lin J. H., Lu N. Y., Manna M., Matsuzaki K., Max L. Berkowitz, Mihajlovic M., Mihajlovic M., Mihajlovic M., Naito A., Nguyen L. T., Pott T., Pott T., Qiu W. H., Raghuraman H., Raghuraman H., Raghuraman H., Raghuraman H., Santo K. P., Sengupta D., Sheeba J. Irudayam, Tobias Pobandt, Torrie G. M., Ulmschneider J. P., Vivcharuk V., Wessman P., Wiedman G., Wimley W. C., Wimley W. C., Yang L., Yeh I. C.   +50 more
core   +3 more sources