TY - JOUR
T1 - Homochiral oligomerization of L-histidine in the presence of liposome membranes
AU - Ishigami, Takaaki
AU - Kaneko, Yoshinori
AU - Suga, Keishi
AU - Okamoto, Yukihiro
AU - Umakoshi, Hiroshi
N1 - Funding Information:
This research was supported by a Japan Society for the Promotion of Science (JSPS) Grant-in-Aid for JSPS Fellows number 13J03878, the Funding Program for Next Generation World-Leading Researchers of the Council for Science and Technology Policy (CSTP) (GR066), a JSPS Grant-in-Aid for Scientific Research A (26249116), and a JSPS Grant-in-Aid for Research Activity Start-up (25889039). One of the authors (T.I.) expresses his gratitude for the Japan Society for the Promotion of Science (JSPS) scholarships. Furthermore, Y.O. acknowledges the Multidisciplinary Research Laboratory System in Osaka University and a Grant-in-Aid for Scientific Research on Innovative Areas “Nanomedicine Molecular Science” (No. 2306) from the Ministry of Education, Culture, Sports, Science and Technology of Japan. All the authors also thank Mr. Makoto Nakata of Peptide Institute, Inc. for performing MALDI-TOF MS experiments.
Publisher Copyright:
© 2015, Springer-Verlag Berlin Heidelberg.
PY - 2015/12/1
Y1 - 2015/12/1
N2 - We report about a novel method for the homochiral oligomerization of l-amino acids in the presence of liposomes. For this homochiral oligomerization, we took advantage of the superior properties of liposomes as chiral adsorbent, concentrator of reacting molecules, and as effective reaction medium. Indeed, liposomes composed of l-phospholipids could enantioselectively bind and concentrate only l-histidine (l-His) on the liposome membrane, and not D-His, which was confirmed by UV measurements. Furthermore, we demonstrate that the liposomes enabled effective oligomerization of l-His on or in the liposome membrane, while the oligomerization of d-His in the liposome system—or in absence of liposomes—was less efficient. The experimental findings are supported by logP value calculations. These calculations indicate that activated intermediates locate in the center of the bilayer where they are protected from hydrolysis due to the hydrophobic environment of the liposome membrane. Therefore, the use of liposomes from l-phospholipids enables homochiral oligomerization and more efficient oligomerization of l-amino acids as compared to d-amino acids. Thus, our developed method could be used for the synthesis of homochiral polymers from racemic mixtures of monomers and may contribute to the understanding of prebiotic biopolymer formation.
AB - We report about a novel method for the homochiral oligomerization of l-amino acids in the presence of liposomes. For this homochiral oligomerization, we took advantage of the superior properties of liposomes as chiral adsorbent, concentrator of reacting molecules, and as effective reaction medium. Indeed, liposomes composed of l-phospholipids could enantioselectively bind and concentrate only l-histidine (l-His) on the liposome membrane, and not D-His, which was confirmed by UV measurements. Furthermore, we demonstrate that the liposomes enabled effective oligomerization of l-His on or in the liposome membrane, while the oligomerization of d-His in the liposome system—or in absence of liposomes—was less efficient. The experimental findings are supported by logP value calculations. These calculations indicate that activated intermediates locate in the center of the bilayer where they are protected from hydrolysis due to the hydrophobic environment of the liposome membrane. Therefore, the use of liposomes from l-phospholipids enables homochiral oligomerization and more efficient oligomerization of l-amino acids as compared to d-amino acids. Thus, our developed method could be used for the synthesis of homochiral polymers from racemic mixtures of monomers and may contribute to the understanding of prebiotic biopolymer formation.
KW - Amino acids
KW - Enantioselective adsorption
KW - Histidine
KW - Homochiral oligomerization
KW - Liposome membrane
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U2 - 10.1007/s00396-015-3764-8
DO - 10.1007/s00396-015-3764-8
M3 - Article
AN - SCOPUS:84949097916
VL - 293
SP - 3649
EP - 3653
JO - Colloid and Polymer Science
JF - Colloid and Polymer Science
SN - 0303-402X
IS - 12
ER -