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Related Concept Videos

Peptide Bonds02:43

Peptide Bonds

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A peptide bond covalently attaches amino acids through a dehydration reaction. One amino acid's carboxyl group and another amino acid's amino group combine, releasing a water molecule. The resulting bond is the peptide bond. The products that such linkages form are peptides. As more amino acids join this growing chain, the resulting chain is a polypeptide. Each polypeptide has a free amino group at one end. This end has the N-terminal, or the amino-terminal, and the other end has a free...
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Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
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Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
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Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
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Chemical reactions directed Peptide self-assembly.

Dnyaneshwar B Rasale1, Apurba K Das2

  • 1Department of Chemistry, Indian Institute of Technology Indore, Khandwa Road, Indore 452017, India. db.rasale@iiti.ac.in.

International Journal of Molecular Sciences
|May 19, 2015
PubMed
Summary

This review explores chemical reaction-mediated peptide self-assembly for creating nanostructures. It highlights how enzymes, native chemical ligation, and photochemical reactions enable precise control over peptide self-assembly for biomedical applications.

Keywords:
chemical reactionenzymenative chemical ligationpeptideself-assembly

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Area of Science:

  • Nanoscience and Nanotechnology
  • Biomedicine
  • Materials Science

Background:

  • Self-assembled nanostructures are crucial in nanoscience and nanotechnology.
  • Self-assembled soft materials are of significant interest for biomedical applications.
  • Small molecules offer a bottom-up approach to tune soft material properties.

Purpose of the Study:

  • To review chemical reaction-mediated peptide self-assembly.
  • To highlight the impact of peptide self-assembly in biology.
  • To explore the use of enzymes, native chemical ligation, and photochemical reactions in peptide self-assembly.

Main Methods:

  • Review of literature on peptide self-assembly.
  • Focus on chemical reaction-mediated strategies.
  • Emphasis on enzymatic, native chemical ligation, and photochemical approaches.

Main Results:

  • Peptide-based self-assembly offers unique features like biocompatibility and tunable side-chain functionality.
  • Chemical reactions provide effective control over peptide self-assembly processes.
  • Enzymes, native chemical ligation, and photochemistry are key tools for directed peptide self-assembly.

Conclusions:

  • Chemical reaction-mediated self-assembly is a powerful strategy for fabricating peptide-based nanostructures.
  • These methods offer precise control for developing advanced materials with potential biomedical applications.
  • Peptide self-assembly, guided by chemical reactions, holds significant promise in nanotechnology and biology.