Selective formation of AAB- and ABC-type heterotrimeric alpha-helical coiled coils

Chemistry : a European Journal
T KiyokawaT Tanaka

Abstract

The alpha-helical coiled coils have a representative amino acid sequence of (abcdefg)(n) heptad repeats. We previously reported that two peptides named IZ-2A and IZ-2W formed an (IZ-2A)(2)/IZ-2W heterotrimer with an Ala-Ala-Trp interaction in the hydrophobic core. In this paper, we describe the selective formation of AAB- and ABC-type heterotrimers. To increase the selectivity of the AAB-type heterotrimeric formation, Lys residues at the f position were mutated to either an Ala or a Gln residue to form IZ-2A(fA) or IZ-2W(fQ). Separately, both IZ-2A(fA) and IZ-2W(fQ) have a random structure at pH 7 and 20 degrees C. However, together IZ-2A(fA) and IZ-2W(fQ) form a 2:1 complex with a thermal transition midpoint (Tm) of 48 degrees C. This procedure was applied to prepare the ABC-type heterotrimer, in which two sets of Ala-Ala-Trp interactions were designed in the hydrophobic core. Interhelical interaction between the e and g positions and the alpha-helical propensity of the amino acid at the f position were also considered in the design. The resultant three peptides selectively formed the ABC-type heterotrimer with a Tm of 51 degrees C. Other peptide combinations had random coil properties.

Citations

Nov 5, 2014·The Journal of Cell Biology·Stephen R NorrisKristen J Verhey
Jul 26, 2006·Chemistry : a European Journal·Satoshi YuzawaToshiki Tanaka
Dec 31, 2008·Chemistry : a European Journal·Toshihisa MizunoToshiki Tanaka
Dec 1, 2005·The Journal of Peptide Research : Official Journal of the American Peptide Society·Y SakuraiT Tanaka
Mar 4, 2020·Nature Chemistry·Audrey E TolbertVincent L Pecoraro
Nov 10, 2010·Langmuir : the ACS Journal of Surfaces and Colloids·Ayumi KashiwadaKiyomi Matsuda
Oct 28, 2004·Journal of the American Chemical Society·Toshiki TanakaMasahiro Shirakawa
Jan 5, 2006·Journal of the American Chemical Society·Nicholas C Yoder, Krishna Kumar

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