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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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Ligand Binding Sites02:40

Ligand Binding Sites

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Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
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Signal Sequences and Sorting Receptors01:41

Signal Sequences and Sorting Receptors

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Signal sequences are short amino acid sequences that guide newly synthesized proteins to their proper location within the cell. Classical signal sequences are fifteen to sixty amino acids long and present at the N-terminus of a polypeptide chain. Each signal sequence has a conserved segment of basic residues towards their N terminus, a hydrophobic core, and a C-terminus rich in polar residues. The C-terminus also contains a signal cleavage site and features a -3 -1 sequence motif. The -3-1...
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A Tripeptide-Stabilized Nanoemulsion of Oleic Acid
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Solid-Binding Peptides in Biomedicine.

Andrew Care1, Peter L Bergquist2,3,4, Anwar Sunna5,6

  • 1Department of Chemistry and Biomolecular Sciences, Macquarie University, North Ryde, NSW, Australia.

Advances in Experimental Medicine and Biology
|October 30, 2017
PubMed
Summary

Solid-binding peptides (SBPs) are versatile tools in nanobiotechnology, enabling the functionalization of nanomaterials. These peptides offer precise control for biomedical applications by selectively binding to inorganic surfaces.

Keywords:
BioconjugationBiomaterialsBiomedicineFunctionalizationSolid-binding peptides

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Area of Science:

  • Nanobiotechnology
  • Materials Science
  • Biomedical Engineering

Background:

  • Solid-binding peptides (SBPs) are increasingly utilized as molecular building blocks in nanobiotechnology.
  • SBPs exhibit high affinity and selectivity for diverse inorganic surfaces, including metals, oxides, semiconductors, and minerals.

Purpose of the Study:

  • To describe Solid-binding peptides (SBPs) and their role in nanobiotechnology.
  • To highlight the potential applications of SBPs in biomedicine, focusing on nanomaterial functionalization.

Main Methods:

  • Review of literature on Solid-binding peptides (SBPs) and their applications.
  • Analysis of SBP capabilities in nanomaterial synthesis, assembly, and functionalization.

Main Results:

  • SBPs facilitate bioconjugation, enhancing biocompatibility and controlling the orientation of nanoscale entities on solid supports.
  • SBPs are employed in controlled nanomaterial synthesis, hybrid biomaterial formation, and protein immobilization.

Conclusions:

  • Solid-binding peptides (SBPs) offer a versatile platform for advanced nanobiotechnological applications.
  • SBPs hold significant potential for developing novel diagnostic and therapeutic nanomaterials for biomedicine.