Journal
ACS APPLIED MATERIALS & INTERFACES
Volume 10, Issue 29, Pages 24349-24360Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acsami.8b00246
Keywords
amphiphilic peptide; DNA condensation; self-assembly; virus-mimicking; gene delivery; molecular simulation
Funding
- National Natural Science Foundation of China [21473255, 21304017, 21773310]
- Fundamental Research Funds for the Central Universities [17CX02050]
- Key Laboratory of Applied Surface and Colloid Chemistry (Shaanxi Normal University)
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A series of surfactant-like peptides have been designed for inducing DNA condensation, which are all comprised of the same set of amino acids in different sequences. Results from experiments and molecular dynamics simulations show that the peptide's self-assembly and DNA-interaction behaviors can be well manipulated through sequence variation. With optimized pairing modes between the beta-sheets, the peptide of I(3)V(3)A(3)G(3)K(3) can induce efficient DNA condensation into virus-mimicking structures. The condensation involves two steps; the peptide molecules first bind onto the DNA chain through electrostatic interactions and then self-associate into beta-sheets under hydrophobic interactions and hydrogen bonding. In such condensates, the peptide beta-sheets act as scaffolds to assist the ordered arrangement of DNA, mimicking the very nature of the virus capsid in helping DNA packaging. Such a hierarchy affords an extremely stable structure to attain the highly condensed state and protect DNA against enzymatic degradation. Moreover, the condensate size can be well tuned by the DNA length. The condensates with smaller sizes and narrow size distribution can deliver DNA efficiently into cells. The study helps not only for probing into the DNA packaging mechanism in virus but also delineating the role of peptide self-assembly in DNA condensation, which may lead to development of peptide-based gene vectors for therapeutic applications.
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