Issue 8, 2013
From the journal:

Molecular BioSystems

Multivalency amplifies the selection and affinity of bradykinin-derived peptides for lipid nanovesicles†

Jonel P. Saludes,*ab   Leslie A. Morton,a   Sara K. Coulup,a   Zeno Fiorini,a   Brandan M. Cook,b   Lida Beninson,c   Edwin R. Chapman,d   Monika Fleshnerc  and  Hang Yin*a  

* Corresponding authors

a Department of Chemistry & Biochemistry and BioFrontiers Institute, University of Colorado, Boulder, CO 80309, USA
E-mail: hubert.yin@colorado.edu

b Department of Chemistry, Washington State University, Pullman, WA 99164, USA
E-mail: jonel.saludes@wsu.edu

c Department of Integrative Physiology, University of Colorado, Boulder, CO 80309, USA

d Howard Hughes Medical Institute and Department of Neuroscience, University of Wisconsin, Madison, WI 53706, USA

Abstract

The trimer of a bradykinin derivative displayed a more than five-fold increase in binding affinity for phosphatidylserine-enriched nanovesicles as compared to its monomeric precursor. The nanovesicle selection is directly correlated with multivalency, which amplifies the electrostatic attraction. This strategy may lead to the development of novel molecular probes for detecting highly curved membrane bilayers.

Graphical abstract: Multivalency amplifies the selection and affinity of bradykinin-derived peptides for lipid nanovesicles

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Article information

DOI
https://doi.org/10.1039/C3MB70109C
Article type
Communication
Submitted
16 Mar 2013
Accepted
08 May 2013
First published
09 May 2013

Mol. BioSyst., 2013,9, 2005-2009

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Multivalency amplifies the selection and affinity of bradykinin-derived peptides for lipid nanovesicles

J. P. Saludes, L. A. Morton, S. K. Coulup, Z. Fiorini, B. M. Cook, L. Beninson, E. R. Chapman, M. Fleshner and H. Yin, Mol. BioSyst., 2013, 9, 2005 DOI: 10.1039/C3MB70109C

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