Mechanisms of Antimicrobial, Cytolytic, and Cell-Penetrating Peptides: From Kinetics to Thermodynamics Export

@article{citeulike:5375421, abstract = {PMID: 19655791 The mechanisms of six different antimicrobial, cytolytic, and cell-penetrating peptides, including some of their variants, are discussed and compared. The specificity of these polypeptides varies; however, they all form amphipathic α-helices when bound to membranes, and there are no striking differences in their sequences. We have examined the thermodynamics and kinetics of their interaction with phospholipid vesicles, namely, binding and peptide-induced dye efflux. The thermodynamics of binding calculated using the Wimley−White interfacial hydrophobicity scale are in good agreement with the values derived from experiment. The generally accepted view that binding affinity determines functional specificity is also supported by experiments in model membranes. We now propose the hypothesis that it is the thermodynamics of the insertion of the peptide into the membrane, from a surface-bound state, that determine the mechanism.}, author = {Almeida, Paulo F. and Pokorny, Antje}, citeulike-article-id = {5375421}, citeulike-linkout-0 = {http://dx.doi.org/10.1021/bi900914g}, citeulike-linkout-1 = {http://pubs.acs.org/doi/abs/10.1021/bi900914g}, day = {1}, doi = {10.1021/bi900914g}, journal = {Biochemistry}, keywords = {almeid09pdf, antimicrobial, cell-penetration, cytolytic, peptides}, month = {September}, number = {34}, pages = {8083--8093}, posted-at = {2009-08-05 23:56:13}, priority = {2}, title = {Mechanisms of Antimicrobial, Cytolytic, and Cell-Penetrating Peptides: From Kinetics to Thermodynamics}, url = {http://dx.doi.org/10.1021/bi900914g}, volume = {48}, year = {2009} }

TY - JOUR ID - citeulike:5375421 L3 - citeulike-article-id:5375421 N2 - PMID: 19655791 The mechanisms of six different antimicrobial, cytolytic, and cell-penetrating peptides, including some of their variants, are discussed and compared. The specificity of these polypeptides varies; however, they all form amphipathic α-helices when bound to membranes, and there are no striking differences in their sequences. We have examined the thermodynamics and kinetics of their interaction with phospholipid vesicles, namely, binding and peptide-induced dye efflux. The thermodynamics of binding calculated using the Wimley−White interfacial hydrophobicity scale are in good agreement with the values derived from experiment. The generally accepted view that binding affinity determines functional specificity is also supported by experiments in model membranes. We now propose the hypothesis that it is the thermodynamics of the insertion of the peptide into the membrane, from a surface-bound state, that determine the mechanism. IS - 34 JF - Biochemistry EP - 8093 TI - Mechanisms of Antimicrobial, Cytolytic, and Cell-Penetrating Peptides: From Kinetics to Thermodynamics VL - 48 SP - 8083 KW - almeid09pdf KW - antimicrobial KW - cell-penetration KW - cytolytic KW - peptides AU - Almeida, Paulo AU - Pokorny, Antje PY - 2009/09/01/ UR - http://dx.doi.org/10.1021/bi900914g ER -