I have a peptide that I am immobilizing onto an SPR chip via His tag. I am concerned that if the His6 sequence is placed right next to the binding sequence, steric hindrances will prevent analyte interactions. However, a spacer sequence should prevent this from happening. Also, is there a substantial difference if the His tag is placed at the C or N terminus of the peptide?
Dear John
You should try to use some of short Peg amino acid or aminohexanoic acid as a spacer instead of spacer sequence.
best
Adam
Dear John,
How about oligoproline spacer? You can see our publication.
Biselectivity of isoDGR peptides for fibronectin binding integrin subtypes a5b1 and avb6: conformational control through flanking amino acids, J. Med. Chem., 4, 1509 - 1519 (2013), DOI:10.1021/jm301221x.
best regards,
Uday.
I would suggest a short Glycine-Serine repeat (we use GSGSGS) to provide flexibility and low hindrance.
polyproline spacers were used some time ago to provide peptides in which some residues were at fixed distances. this was to do some fundamental studies. see for instance J Am Chem Soc. 2004 Nov 3;126(43):13888-9.; Acta Biochim Pol. 1997;44(4):627-44.; Curr Opin Chem Biol. 2008 Dec;12(6):755-9. doi: 10.1016/j.cbpa.2008.08.026.
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