Adv Polym Sci (2013) 259: 159–200
DOI: 10.1007/12_2013_221
© Springer-Verlag Berlin Heidelberg 2013
Published online: 27 August 2013
Ordering of Polypeptides in Liquid Crystals,
Gels and Micelles
Chunhua Cai, Jiaping Lin, Zeliang Zhuang, and Wenjie Zhu
Abstract Ordered structures assembled from polypeptides have attracted a great
deal of attention over the past few decades. Both α-helix and β-sheet conformations
of polypeptides support the formation of ordered structures during the assembly
process. For polypeptides with α-helix conformation, the ordered structures are
formed mainly by side-by-side packing of α-helix rods. For polypeptides with
β-sheet conformation, ordering of the chains can be achieved by parallel or antiparallel packing. The ordering characteristic of polypeptide chains gives rise to
fascinating assembly behaviors of polypeptide homopolymers and copolymers in
solution. Usually, a decrease in polymer concentration is accompanied by the
assembly of polypeptides into liquid crystals (LCs), gels, and micelles. This review
describes the ordering structures of polypeptides in these assemblies. In LC
structures, polypeptide homopolymer chains are packed in a highly ordered fashion
with smectic, nematic, and cholesteric phases. Both polypeptide homopolymers and
copolymers support the formation of gels in solution. The dislocated side-by-side
packing of polypeptide helices is the basic ordering characteristic of the
polypeptides in gels. Compared with the α-helix conformation, gels formed from
polypeptides with β-sheet conformation show higher stability. In dilute solutions,
amphiphilic polypeptide copolymers can self-assemble into micelles that include
cylinders, vesicles, and complex hierarchical structures. The ordering nature of the
polypeptide chains can be observed in the assemblies. The close relationship with
proteins makes polypeptides and their assembly structures ideal models for protein
research and promising candidates in biorelated applications.
Keywords Gels Á Liquid crystals Á Micelles Á Ordered structure Á Polypeptide Á
Self-assembly
C. Cai, J. Lin (*), Z. Zhuang, and W. Zhu
Shanghai Key Laboratory of Advanced Polymeric Materials, Key Laboratory for Ultrafine
Materials of Ministry of Education, School of Materials Science and Engineering, East China
University of Science and Technology, Shanghai 200237, China
e-mail: jlin@ecust.edu.cn
DOI: 10.1007/12_2013_221
© Springer-Verlag Berlin Heidelberg 2013
Published online: 27 August 2013
Ordering of Polypeptides in Liquid Crystals,
Gels and Micelles
Chunhua Cai, Jiaping Lin, Zeliang Zhuang, and Wenjie Zhu
Abstract Ordered structures assembled from polypeptides have attracted a great
deal of attention over the past few decades. Both α-helix and β-sheet conformations
of polypeptides support the formation of ordered structures during the assembly
process. For polypeptides with α-helix conformation, the ordered structures are
formed mainly by side-by-side packing of α-helix rods. For polypeptides with
β-sheet conformation, ordering of the chains can be achieved by parallel or antiparallel packing. The ordering characteristic of polypeptide chains gives rise to
fascinating assembly behaviors of polypeptide homopolymers and copolymers in
solution. Usually, a decrease in polymer concentration is accompanied by the
assembly of polypeptides into liquid crystals (LCs), gels, and micelles. This review
describes the ordering structures of polypeptides in these assemblies. In LC
structures, polypeptide homopolymer chains are packed in a highly ordered fashion
with smectic, nematic, and cholesteric phases. Both polypeptide homopolymers and
copolymers support the formation of gels in solution. The dislocated side-by-side
packing of polypeptide helices is the basic ordering characteristic of the
polypeptides in gels. Compared with the α-helix conformation, gels formed from
polypeptides with β-sheet conformation show higher stability. In dilute solutions,
amphiphilic polypeptide copolymers can self-assemble into micelles that include
cylinders, vesicles, and complex hierarchical structures. The ordering nature of the
polypeptide chains can be observed in the assemblies. The close relationship with
proteins makes polypeptides and their assembly structures ideal models for protein
research and promising candidates in biorelated applications.
Keywords Gels Á Liquid crystals Á Micelles Á Ordered structure Á Polypeptide Á
Self-assembly
C. Cai, J. Lin (*), Z. Zhuang, and W. Zhu
Shanghai Key Laboratory of Advanced Polymeric Materials, Key Laboratory for Ultrafine
Materials of Ministry of Education, School of Materials Science and Engineering, East China
University of Science and Technology, Shanghai 200237, China
e-mail: jlin@ecust.edu.cn