Title

Investigation of Methanobactin and Its Analog Peptides

Document Type

Thesis

Degree Name

Master of Science (MS)

Department

Chemistry

Date of Award

Fall 2013

Abstract

Methanotrophs are the group of microorganisms that utilize methane as their sole carbon and energy source. Methanobactins (mb) are a class of low molecular mass copper binding chromopeptides analogous to pyoverdin class iron-binding siderophores, secreted by methanotrophs, with high binding affinity to Cu (II) and other metal ions and are hypothesized to mediate copper acquisition from the environment of methanotrophs. Proteins have built up different ways to bind to other molecules to perform their essential functions like protein-protein and protein-nucleic acid interactions. Zinc-binding repeated units, known as zinc fingers (ZnF) are short peptide sequence motifs characterized by the co-ordination of Zn(II), which stabilizes the finger like folding. In addition, various classes of ZnF proteins were synthetically produced which display versatility in both structure and function. ac-His-Cys-Gly-Pro-His-Cys (ac-HCGPHC) is a zinc finger-like peptide synthesized with an insight to comprise of both methanobactin and zinger finger properties. The structural importance of the disulfide linkage for metal binding of methanobactin at various pH and different experimental conditions has been studied and a binding profile of methanobactin developed. The binding properties of ac-HCGPHC has been studied in comparison to methanobactin and the relative pH dependent binding affinities of Mn(II), Co(II), Ni(II), Zn(II) and Cu(II) and the collision cross section areas of the various species determined.

Advisor

Laurence Angel

Subject Categories

Chemistry | Physical Sciences and Mathematics

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