Adsorption and conformation change of short helical peptides on silica and aluminosilicate surfaces

Motivated by the challenges in understanding important features of protein adsorption, the interactions between (-helical peptides and a carefully selected set of model surfaces were studied. The peptide sequences contained three blocks of two to five residues each, with the side chains of the N-terminal and C-terminal blocks having negative and positive charges, respectively, and the central block having uncharged side chains. The conformation of a variety of such peptides was studied in solution by circular dichroism (CD) and H nuclear magnetic resonance (NMR) spectroscopy, in order to characterize the degree of xc-helicity in solution, as a function of temperature, pH, and chemical denaturant (urea) concentration. Intramolecular electrostatic interactions arising from the charged side chains, together with the central block of gc-helix-forming alanine residues, were found to stabilize oc-helicity. These interactions were balanced by the natural tendency toward disordered structures, which resulted in fractional oc-helicities between 25% and 50% when in solution. Adsorption isotherms for the peptide Ac-DDDDAAYAARRRR-Am on amorphous colloidal silica nanoparticles were studied in detail. A greater amount of peptide was adsorbed at basic pH than at neutral pH. The was fit with Langmuir and Frumkin isotherms, and the free energy, enthalpy, and entropy of adsorption were calculated. The enthalpy of adsorption at pH 9 (-17 kJ mol'1) was consistent with calculations of the electrostatic interaction between the screened silica surface charge and the dipolar charge distribution on the peptide arising from the charged side chains.

Department dc:contributor.department

Massachusetts Institute of Technology. Dept. of Materials Science and Engineering.

Grantor dc:publisher

Massachusetts Institute of Technology

Year dc:date.issued

2002

Author dc:creator

• Read, Michael J. (Michael Joseph), 1975-

Advisor dc:contributor.advisor

• Sandra L. Burkett and Anne M. Mayes.

• Materials Science and Engineering.

Statement dc:rights

• M.I.T. theses are protected by copyright. They may be viewed from this source for any purpose, but reproduction or distribution in any format is prohibited without written permission. See provided URL for inquiries about permission.

Licence dc:rights.uri

• http://dspace.mit.edu/handle/1721.1/7582

Language dc:language.iso

eng

Handle dc:identifier.uri

http://hdl.handle.net/1721.1/29914

OAI identifier oai:identifier

oai:dspace.mit.edu:1721.1/29914