TY - JOUR
T1 - A tubular biocontainer
T2 - Metal ion-induced 1D assembly of a molecularly engineered chaperonin
AU - Biswas, Shuvendu
AU - Kinbara, Kazushi
AU - Oya, Nobuhiro
AU - Ishii, Noriyuki
AU - Taguchi, Hideki
AU - Aida, Takuzo
PY - 2009/6/10
Y1 - 2009/6/10
N2 - (Figure Presented) GroELSP/MC, prepared by genetic and chemical modifications of group I chaperonin protein GroEL, site-specifically possesses ∼28 photochromic (spiropyran [SP] and merocyanine [MC]) units in the entrance parts of its cavity. Addition of divalent metal ions such as Mg 2+ to a tris-HCl buffer solution of GroELSP/MC results in one-dimensional (1D) assembly of GroELSP/MC, affording cylindrical hollow fibers with a very large aspect ratio; the longest fiber was ∼2.5 μm long, corresponding to a 170-mer of GroELSP/MC (MW ≈ 1.4 × 108). When such long fibers are mixed with EDTA, they are cut into short-chain oligomers and eventually into monomeric GroELSP/MC. Similar to GroEL, GroELSP/MC possesses a large binding affinity toward denatured proteins. When GroELSP/MC undergoes 1D assembly after incubation with a denatured protein, guest-containing cylindrical fibers result.
AB - (Figure Presented) GroELSP/MC, prepared by genetic and chemical modifications of group I chaperonin protein GroEL, site-specifically possesses ∼28 photochromic (spiropyran [SP] and merocyanine [MC]) units in the entrance parts of its cavity. Addition of divalent metal ions such as Mg 2+ to a tris-HCl buffer solution of GroELSP/MC results in one-dimensional (1D) assembly of GroELSP/MC, affording cylindrical hollow fibers with a very large aspect ratio; the longest fiber was ∼2.5 μm long, corresponding to a 170-mer of GroELSP/MC (MW ≈ 1.4 × 108). When such long fibers are mixed with EDTA, they are cut into short-chain oligomers and eventually into monomeric GroELSP/MC. Similar to GroEL, GroELSP/MC possesses a large binding affinity toward denatured proteins. When GroELSP/MC undergoes 1D assembly after incubation with a denatured protein, guest-containing cylindrical fibers result.
UR - http://www.scopus.com/inward/record.url?scp=67650523187&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=67650523187&partnerID=8YFLogxK
U2 - 10.1021/ja902696q
DO - 10.1021/ja902696q
M3 - Article
C2 - 19489642
AN - SCOPUS:67650523187
VL - 131
SP - 7556
EP - 7557
JO - Journal of the American Chemical Society
JF - Journal of the American Chemical Society
SN - 0002-7863
IS - 22
ER -