Probing the molecular mechanisms of quartz-binding peptides

Ersin Emre Oren, Rebecca Notman, Il Won Kim, John Evans, Tiffany R. Walsh, Ram Samudrala, Candan Tamerler, Mehmet Sarikaya

Research output: Contribution to journalArticle

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 (100) 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.

Original languageEnglish (US)
Pages (from-to)11003-11009
Number of pages7
JournalLangmuir
Volume26
Issue number13
DOIs
StatePublished - Jul 6 2010

Fingerprint

Quartz
Peptides
peptides
quartz
Molecular recognition
Biomineralization
synthesizers
biotechnology
inorganic materials
Surface diffusion
Dichroism
Biotechnology
nanotechnology
surface diffusion
Binding energy
biology
medicine
Nanotechnology
statistical analysis
dichroism

ASJC Scopus subject areas

  • Electrochemistry
  • Condensed Matter Physics
  • Surfaces and Interfaces
  • Materials Science(all)
  • Spectroscopy

Cite this

Oren, E. E., Notman, R., Kim, I. W., Evans, J., Walsh, T. R., Samudrala, R., ... Sarikaya, M. (2010). Probing the molecular mechanisms of quartz-binding peptides. Langmuir, 26(13), 11003-11009. https://doi.org/10.1021/la100049s

Probing the molecular mechanisms of quartz-binding peptides. / Oren, Ersin Emre; Notman, Rebecca; Kim, Il Won; Evans, John; Walsh, Tiffany R.; Samudrala, Ram; Tamerler, Candan; Sarikaya, Mehmet.

In: Langmuir, Vol. 26, No. 13, 06.07.2010, p. 11003-11009.

Research output: Contribution to journalArticle

Oren, EE, Notman, R, Kim, IW, Evans, J, Walsh, TR, Samudrala, R, Tamerler, C & Sarikaya, M 2010, 'Probing the molecular mechanisms of quartz-binding peptides', Langmuir, vol. 26, no. 13, pp. 11003-11009. https://doi.org/10.1021/la100049s
Oren EE, Notman R, Kim IW, Evans J, Walsh TR, Samudrala R et al. Probing the molecular mechanisms of quartz-binding peptides. Langmuir. 2010 Jul 6;26(13):11003-11009. https://doi.org/10.1021/la100049s
Oren, Ersin Emre ; Notman, Rebecca ; Kim, Il Won ; Evans, John ; Walsh, Tiffany R. ; Samudrala, Ram ; Tamerler, Candan ; Sarikaya, Mehmet. / Probing the molecular mechanisms of quartz-binding peptides. In: Langmuir. 2010 ; Vol. 26, No. 13. pp. 11003-11009.
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