Self-Assembly and Hydrogelation of Coil-Sheet Poly(l -lysine)- block-poly(l -threonine) Block Copolypeptides

Sheng-Shu Hou, Nai Shin Fan, Yu Chao Tseng, Jeng-Shiung Jan

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

This study reports the self-assembly and hydrogelation of coil-sheet poly(l-lysine)-block-poly(l-threonine) (PLL-b-PLT) block copolypeptides. Our experiments showed that the PLL-b-PLT block copolypeptides with degrees of polymerization (DPs) between 30 and 60 can self-assemble to form fibrils due to the packing of sheetlike PLT at low polymer concentrations; moreover, further increasing the polymer concentration can result in the formation of transparent hydrogels due to fibril entanglements. The hydrogelation was determined by the orientation and packing of the fibril assemblies, which aremainly dictated by the balance between the intermolecular hydrogen bonding interactions and charge repulsion exerted respectively by sheetlike PLT and positively charged, coil PLL segments. The noncovalent interactions can be manipulated by varying the polypeptide chain length and composition, which would result in these block copolypeptides exhibiting different critical gelation concentrations (CGCs), gel molecular assemblies, and mechanical properties.

Original languageEnglish
Pages (from-to)8054-8063
Number of pages10
JournalMacromolecules
Volume51
Issue number20
DOIs
Publication statusPublished - 2018 Oct 23

Fingerprint

Threonine
Self assembly
Lysine
Polymers
Hydrogels
Polypeptides
Gelation
Phase locked loops
Chain length
Hydrogen bonds
Gels
Polymerization
Mechanical properties
Peptides
Chemical analysis
Experiments

All Science Journal Classification (ASJC) codes

  • Organic Chemistry
  • Polymers and Plastics
  • Inorganic Chemistry
  • Materials Chemistry

Cite this

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title = "Self-Assembly and Hydrogelation of Coil-Sheet Poly(l -lysine)- block-poly(l -threonine) Block Copolypeptides",
abstract = "This study reports the self-assembly and hydrogelation of coil-sheet poly(l-lysine)-block-poly(l-threonine) (PLL-b-PLT) block copolypeptides. Our experiments showed that the PLL-b-PLT block copolypeptides with degrees of polymerization (DPs) between 30 and 60 can self-assemble to form fibrils due to the packing of sheetlike PLT at low polymer concentrations; moreover, further increasing the polymer concentration can result in the formation of transparent hydrogels due to fibril entanglements. The hydrogelation was determined by the orientation and packing of the fibril assemblies, which aremainly dictated by the balance between the intermolecular hydrogen bonding interactions and charge repulsion exerted respectively by sheetlike PLT and positively charged, coil PLL segments. The noncovalent interactions can be manipulated by varying the polypeptide chain length and composition, which would result in these block copolypeptides exhibiting different critical gelation concentrations (CGCs), gel molecular assemblies, and mechanical properties.",
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Self-Assembly and Hydrogelation of Coil-Sheet Poly(l -lysine)- block-poly(l -threonine) Block Copolypeptides. / Hou, Sheng-Shu; Fan, Nai Shin; Tseng, Yu Chao; Jan, Jeng-Shiung.

In: Macromolecules, Vol. 51, No. 20, 23.10.2018, p. 8054-8063.

Research output: Contribution to journalArticle

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AU - Tseng, Yu Chao

AU - Jan, Jeng-Shiung

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AB - This study reports the self-assembly and hydrogelation of coil-sheet poly(l-lysine)-block-poly(l-threonine) (PLL-b-PLT) block copolypeptides. Our experiments showed that the PLL-b-PLT block copolypeptides with degrees of polymerization (DPs) between 30 and 60 can self-assemble to form fibrils due to the packing of sheetlike PLT at low polymer concentrations; moreover, further increasing the polymer concentration can result in the formation of transparent hydrogels due to fibril entanglements. The hydrogelation was determined by the orientation and packing of the fibril assemblies, which aremainly dictated by the balance between the intermolecular hydrogen bonding interactions and charge repulsion exerted respectively by sheetlike PLT and positively charged, coil PLL segments. The noncovalent interactions can be manipulated by varying the polypeptide chain length and composition, which would result in these block copolypeptides exhibiting different critical gelation concentrations (CGCs), gel molecular assemblies, and mechanical properties.

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