Homopolypeptide Vesicles Triggered by Side-Chain Hydration

Xin-Jie Shi; Zhen Liu; Yang-Chun Xie; Min Xu; Xiao-Hua He

doi:10.1007/s10118-022-2784-3

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Homopolypeptide Vesicles Triggered by Side-Chain Hydration

RESEARCH ARTICLE | Updated：2022-11-16

- Homopolypeptide Vesicles Triggered by Side-Chain Hydration
- Chinese Journal of Polymer Science Vol. 40, Issue 12, Pages: 1631-1639(2022)
- Affiliations：
  
  a.School of Chemistry and Molecular Engineering, East China Normal University, Shanghai 200241, China
  b.School of Physics and Electronic Science, Shanghai Key Laboratory of Magnetic Resonance, East China Normal University, Shanghai 200241, China
- Author bio：
  
  xumin@phy.ecnu.edu.cn (M.X.)
  xhhe@chem.ecnu.edu.cn (X.H.H.)
- Funds：
- DOI：10.1007/s10118-022-2784-3
  CLC：
- Received：02 April 2022，
  
  Revised：2022-4-23，
  
  Accepted：05 May 2022，
  
  Online First：10 August 2022，
  
  Published：01 December 2022
- Accepted：
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Shi, X. J.; Liu, Z.; Xie, Y. C.; Xu. M.; He, X. H. Homopolypeptide vesicles triggered by side-chain hydration. Chinese J. Polym. Sci. 2022, 40, 1631–1639

Xin-Jie Shi, Zhen Liu, Yang-Chun Xie, et al. Homopolypeptide Vesicles Triggered by Side-Chain Hydration[J]. Chinese Journal of Polymer Science, 2022, 40(12): 1631-1639.
Shi, X. J.; Liu, Z.; Xie, Y. C.; Xu. M.; He, X. H. Homopolypeptide vesicles triggered by side-chain hydration. Chinese J. Polym. Sci. 2022, 40, 1631–1639 DOI： 10.1007/s10118-022-2784-3.

Xin-Jie Shi, Zhen Liu, Yang-Chun Xie, et al. Homopolypeptide Vesicles Triggered by Side-Chain Hydration[J]. Chinese Journal of Polymer Science, 2022, 40(12): 1631-1639. DOI： 10.1007/s10118-022-2784-3.

摘要

The formation of different polypeptide self-assembly structures including vesicles and micelles is due to their different side-group hydrophilicity

and their self-assembly mechanisms are identified from the molecular level. These findings can be useful to understand how the hydrophilicity of the side chains of polypeptides to control their self-assembling behavior.

Abstract

The formation of homopolypeptide vesicles and the identification of their self-assembly mechanism have been challenging issues in the field of polymer self-assembly. Using complementary circular dichroism (CD)

Fourier transform infrared (FTIR) and low-field nuclear magnetic resonance (LF-NMR) spectroscopies

in this study we show that the higher hydrophilic ability of side-chains is a key factor for the formation of homopolypeptide vesicles from homo poly(

Nε

-carbobenzoxy-L-lysine) (PZlys)

in which the vesicular structures are confirmed by scanning electron microscopy (SEM)

transmission electron microscopy (TEM) and atomic force microscopy (AFM) measurements. Poly(

-benzyl-L-glutamate-

Nε

-carbobenzoxy-L-lysine) [P(BLG-

-Zlys)] containing different molar ratios of BLG to Zlys units with the same peptide backbone as PZlys are used as the controls. The copolypeptides can only form micelles under the same conditions

due to the more hydrophobic nature of their side-chains. These results show that the specific side-chain structure of the polypeptides plays a fundamental role in the self-assembly of homopolypeptides. These findings can be useful to understand how the hydrophilicity of the side chains of amino acid residues on the surface of a protein affects its structures.

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Keywords

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