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Study of NAP adsorption and assembly on the surface of HOPG

Korolkov, Vladimir V.; Allen, Stephanie; Roberts, Clive J.; Gozes, Illana; Tendler, Saul J.B.

Authors

Vladimir V. Korolkov

STEPHANIE ALLEN stephanie.allen@nottingham.ac.uk
Professor of Pharmaceutical Biophysics

Illana Gozes

Saul J.B. Tendler



Abstract

NAP is an octapeptide that has demonstrated a neuroprotective/therapeutic efficacy at very low concentrations in preclinical studies and in a number of clinical trials. Yet little is known about its structural organization at low concentrations. Here, we have employed atomic force microscopy to investigate NAP peptide assembly on graphite in aqueous media at nanomolar concentration. High spatial resolution scans of NAP assemblies reveal their fine structure with clearly resolved single NAP units. This observation leads us to conclude that NAP molecules do not form complex self-assembled structures at nanomolar concentration when adsorbed on graphite surface.

Citation

Korolkov, V. V., Allen, S., Roberts, C. J., Gozes, I., & Tendler, S. J. (2014). Study of NAP adsorption and assembly on the surface of HOPG. Peptides, 62, 55-58. https://doi.org/10.1016/j.peptides.2014.09.017

Journal Article Type Article
Acceptance Date Sep 17, 2014
Online Publication Date Sep 30, 2019
Publication Date 2014-12
Deposit Date Oct 24, 2014
Publicly Available Date Dec 31, 2014
Journal Peptides
Print ISSN 0196-9781
Electronic ISSN 0196-9781
Publisher Elsevier
Peer Reviewed Peer Reviewed
Volume 62
Pages 55-58
DOI https://doi.org/10.1016/j.peptides.2014.09.017
Keywords NAP; Atomic Force Microscopy; davunetide; adsorption; peptides
Public URL http://eprints.nottingham.ac.uk/id/eprint/27680
Publisher URL http://www.sciencedirect.com/science/article/pii/S0196978114002861
Copyright Statement Copyright information regarding this work can be found at the following address: http://eprints.nottingham.ac.uk/end_user_agreement.pdf
Additional Information This article is maintained by: Elsevier; Article Title: Study of NAP adsorption and assembly on the surface of HOPG; Journal Title: Peptides; CrossRef DOI link to publisher maintained version: https://doi.org/10.1016/j.peptides.2014.09.017; Content Type: article; Copyright: Copyright © 2014 Elsevier Inc. All rights reserved.

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