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Polypeptide Conjugate Binders for Protein Recognition
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Biochemistry and Organic Chemistry, Organic Chemistry II.
2007 (English)In: Topics in current chemistry, ISSN 0340-1022, E-ISSN 1436-5049, Vol. 277, 89-106 p.Article, review/survey (Refereed) Published
Abstract [en]

A new class of hybrid molecules for protein recognition is presented, where polypeptides are covalently linked to small organic molecules to form polypeptide conjugates that bind proteins with high affinity and selectivity. To illustrate the concept, a binder for human carbonic anhydrase 11 with a dissociation constant of 4 nM is described. The affinity of the polypeptide conjugate arises from cooperativity in binding between a benzenesulfonamide residue, with a dissociation constant of 1.5 mu M, and the polypeptide scaffold with a dissociation constant of < 1 mM. The combination of a ligand with moderate affinity for a target protein with a polypeptide relaxes considerably the need for high affinity on the part of the polypeptide, and thus the need for structural complexity and preorganization. At the same time, the requirement for high affinity on the part of ligand is relaxed. As a consequence, the time for development of robust, high affinity, selective binder is shortened. The chemical approach to protein recognition provides well-defined molecular entities that are conveniently handled, stored and site-specifically functionalized.

Place, publisher, year, edition, pages
2007. Vol. 277, 89-106 p.
National Category
Organic Chemistry
URN: urn:nbn:se:uu:diva-12013DOI: 10.1007/128_2007_129ISI: 000248621900003OAI: oai:DiVA.org:uu-12013DiVA: diva2:39782
Available from: 2007-11-26 Created: 2007-11-26 Last updated: 2011-03-28Bibliographically approved

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