Journal article

Effect of linker length on avidin binding to biotinylated gramicidin A

Aphrodite Anastasiadis, Craig J Morton, Gert H Talbo, Roger E Koeppe, Frances Separovic

INTERNATIONAL JOURNAL OF PEPTIDE RESEARCH AND THERAPEUTICS | SPRINGER | Published : 2006

Abstract

Biotinylated gramicidins are an important component of the AMBRI® "ion channel switch™" biosensor. These gramicidin A (gA) analogues have a biotin attached to the C-terminus of gA via a number of aminocaproyl linker groups (X). The structure of gA5XB has been determined in deuterated sodium dodecyl sulfate micelles and is similar to native gA and other modified gA analogues. The biotin and aminocaproyl groups were mobile and located in the aqueous phase and when avidin was added, NMR and MS studies showed that gA5XB bound more effectively to avidin than gA2XB. The length and flexibility of the linker appears to be important for biotin-avidin binding and, in the AMBRI® biosensor, gA5XB is a m..

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