Oren, Ersin Emre, Notman, Rebecca, Kim, Il Won, Evans, John Spencer, Walsh, Tiffany R., Samudrala, Ram, Tamerler, Candan and Sarikaya, Mehmet. (2010) Probing the molecular mechanisms of quartz-binding peptides. Langmuir, Vol.26 (No.13). pp. 11003-11009. ISSN 0743-7463

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Abstract

Understanding the mechanisms of biomineralization and the realization of biology-inspired inorganic materials formation largely depends on our ability to manipulate peptide/solid interfacial interactions. Material interfaces and biointerfaces are critical sites for bioinorganic synthesis, surface diffusion, and molecular recognition. Recently adapted biocombinatorial techniques permit the isolation of peptides recognizing inorganic solids that are used as molecular building blocks, for example, as synthesizers, linkers, and assemblers. Despite their ubiquitous utility in nanotechnology, biotechnology, and medicine, the fundamental mechanisms of molecular recognition of engineered peptides binding to inorganic surfaces remain largely unknown. To explore propensity rules connecting sequence, structure, and function that play key roles in peptide/solid interactions, we combine two different approaches: a statistical analysis that searches for highly enriched motifs among de novo designed peptides, and, atomistic simulations of three experimentally validated peptides. The two strong and one weak quartz-binding peptides were chosen for the simulations at the quartz (1 00) surface under aqueous conditions. Solution-based peptide structures were analyzed by circular dichroism measurements. Small and hydrophobic residues, such as Pro, play a key role at the interface by making close contact with the solid and hindering formation of intrapeptide hydrogen bonds. The high binding affinity of a peptide may be driven by a combination of favorable enthalpic and entropic effects, that is, a strong binder may possess a large number of possible binding configurations, many of which having relatively high binding energies. The results signify the role of the local molecular environment among the critical residues that participate in solid binding. The work herein describes molecular conformations inherent in material-specific peptides and provides fundamental insight into the atomistic understanding of peptide/solid interfaces.

Item Type:	Journal Article
Subjects:	Q Science > QD Chemistry Q Science > QP Physiology T Technology > TA Engineering (General). Civil engineering (General)
Divisions:	Faculty of Science > Chemistry Faculty of Science > Centre for Scientific Computing
Library of Congress Subject Headings (LCSH):	Biomineralization, Bioinorganic chemistry, Peptides -- Synthesis, Nanostructured materials
Journal or Publication Title:	Langmuir
Publisher:	American Chemical Society
ISSN:	0743-7463
Date:	6 July 2010
Volume:	Vol.26
Number:	No.13
Number of Pages:	7
Page Range:	pp. 11003-11009
Identification Number:	10.1021/la100049s
Status:	Peer Reviewed
Publication Status:	Published
Access rights to Published version:	Restricted or Subscription Access
Funder:	National Science Foundation (U.S.). Materials Research Science and Engineering Centers (Program), Engineering and Physical Sciences Research Council (EPSRC), National Science Foundation (U.S.) (NSF)
Grant number:	EP/E02095X/1 (EPSRC)
URI:	http://wrap.warwick.ac.uk/id/eprint/5604

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