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Molecular design principles of Lysine-DOPA wet adhesion

Author

Listed:
  • Yiran Li

    (University of California
    Nanjing University)

  • Jing Cheng

    (University of California)

  • Peyman Delparastan

    (University of California)

  • Haoqi Wang

    (Nanjing University)

  • Severin J. Sigg

    (University of California)

  • Kelsey G. DeFrates

    (University of California)

  • Yi Cao

    (Nanjing University)

  • Phillip B. Messersmith

    (University of California
    Lawrence Berkeley National Laboratory)

Abstract

The mussel byssus has long been a source of inspiration for the adhesion community. Recently, adhesive synergy between flanking lysine (Lys, K) and 3,4-Dihydroxyphenylalanine (DOPA, Y) residues in the mussel foot proteins (Mfps) has been highlighted. However, the complex topological relationship of DOPA and Lys as well as the interfacial adhesive roles of other amino acids have been understudied. Herein, we study adhesion of Lys and DOPA-containing peptides to organic and inorganic substrates using single-molecule force spectroscopy (SMFS). We show that a modest increase in peptide length, from KY to (KY)3, increases adhesion strength to TiO2. Surprisingly, further increase in peptide length offers no additional benefit. Additionally, comparison of adhesion of dipeptides containing Lys and either DOPA (KY) or phenylalanine (KF) shows that DOPA is stronger and more versatile. We furthermore demonstrate that incorporating a nonadhesive spacer between (KY) repeats can mimic the hidden length in the Mfp and act as an effective strategy to dissipate energy.

Suggested Citation

  • Yiran Li & Jing Cheng & Peyman Delparastan & Haoqi Wang & Severin J. Sigg & Kelsey G. DeFrates & Yi Cao & Phillip B. Messersmith, 2020. "Molecular design principles of Lysine-DOPA wet adhesion," Nature Communications, Nature, vol. 11(1), pages 1-8, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-17597-4
    DOI: 10.1038/s41467-020-17597-4
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    Cited by:

    1. Zhengyu Xu & Jiajun Lu & Di Lu & Yiran Li & Hai Lei & Bin Chen & Wenfei Li & Bin Xue & Yi Cao & Wei Wang, 2024. "Rapidly damping hydrogels engineered through molecular friction," Nature Communications, Nature, vol. 15(1), pages 1-11, December.
    2. Chongrui Zhang & Xufei Liu & Jiang Gong & Qiang Zhao, 2023. "Liquid sculpture and curing of bio-inspired polyelectrolyte aqueous two-phase systems," Nature Communications, Nature, vol. 14(1), pages 1-10, December.
    3. Yuhe Shen & Rongxin Su & Dongzhao Hao & Xiaojian Xu & Meital Reches & Jiwei Min & Heng Chang & Tao Yu & Qing Li & Xiaoyu Zhang & Yuefei Wang & Yuefei Wang & Wei Qi, 2023. "Enzymatic polymerization of enantiomeric L−3,4-dihydroxyphenylalanine into films with enhanced rigidity and stability," Nature Communications, Nature, vol. 14(1), pages 1-13, December.
    4. Bin Xue & Jie Gu & Lan Li & Wenting Yu & Sheng Yin & Meng Qin & Qing Jiang & Wei Wang & Yi Cao, 2021. "Hydrogel tapes for fault-tolerant strong wet adhesion," Nature Communications, Nature, vol. 12(1), pages 1-12, December.
    5. Wonjun Yim & Zhicheng Jin & Yu-Ci Chang & Carlos Brambila & Matthew N. Creyer & Chuxuan Ling & Tengyu He & Yi Li & Maurice Retout & William F. Penny & Jiajing Zhou & Jesse V. Jokerst, 2024. "Polyphenol-stabilized coacervates for enzyme-triggered drug delivery," Nature Communications, Nature, vol. 15(1), pages 1-11, December.
    6. Donghui Zhang & Jingjing Liu & Qi Chen & Weinan Jiang & Yibing Wang & Jiayang Xie & Kaiqian Ma & Chao Shi & Haodong Zhang & Minzhang Chen & Jianglin Wan & Pengcheng Ma & Jingcheng Zou & Wenjing Zhang , 2021. "A sandcastle worm-inspired strategy to functionalize wet hydrogels," Nature Communications, Nature, vol. 12(1), pages 1-14, December.

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