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Amino acids03:42

Amino acids

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Amino acids are the monomers that comprise proteins. Each amino acid has the same fundamental structure, which consists of a central carbon atom, or the alpha (α) carbon, bonded to an amino group (NH2), a carboxyl group (COOH), and to a hydrogen atom. Every amino acid also has another atom or group of atoms bonded to the central atom known as the R group. There are 20 common amino acids present in proteins, each with a different R group. Variation in the amino acid sequence is responsible for...
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Protein Organization01:13

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Protein Organization01:24

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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.
The primary structure of a protein is its amino acid sequence....
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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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What are Proteins?

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Proteins are polymers of amino acids linked together by peptide bonds. Proteins and polypeptides are interchangeably used to refer to long chains of amino acids. However, polypeptides have a molecular weight of fewer than 10,000 daltons, while proteins have greater molecular weight.  Polypeptides with less than 20 amino acids are called oligopeptides or simply peptides. Interactions among the constituent amino acid side chains of proteins help them fold into a stable 3-dimensional...
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Split-and-pool Synthesis and Characterization of Peptide Tertiary Amide Library
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γ-AApeptides: Design, Structure, and Applications.

Yan Shi1, Peng Teng1, Peng Sang1

  • 1Department of Chemistry, University of South Florida , 4202 East Fowler Ave, Tampa, Florida 33620, United States.

Accounts of Chemical Research
|February 23, 2016
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Summary
This summary is machine-generated.

γ-AApeptides, a novel class of peptidomimetics, mimic peptide structures and functions while resisting degradation. These versatile molecules show potential in cell penetration, targeting specific cell surface receptors, and combating drug-resistant bacteria and Alzheimer's disease.

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Area of Science:

  • Chemical Biology
  • Medicinal Chemistry
  • Biomaterials Science

Background:

  • Peptidomimetics offer enhanced stability and bioavailability compared to natural peptides.
  • The potential of peptide nucleic acid (PNA) backbones for mimicking peptide structures remained largely unexplored.
  • A novel class of peptidomimetics, γ-AApeptides, was developed using a chiral γ-PNA backbone.

Purpose of the Study:

  • To explore the synthesis, structure, and biological applications of γ-AApeptides.
  • To investigate the potential of γ-AApeptides as mimics of bioactive peptides.
  • To evaluate the therapeutic and diagnostic potential of γ-AApeptides.

Main Methods:

  • Solid-phase synthesis of linear and cyclic γ-AApeptides.
  • Mimicry studies of Tat, RGD, and fMLF peptides.
  • Secondary structure analysis (helical, β-turn-like structures).
  • Antimicrobial activity assays against drug-resistant bacteria.
  • Combinatorial screening for inhibition of Aβ40 aggregation.
  • Identification of STAT3/DNA interaction modulators.

Main Results:

  • γ-AApeptides are resistant to proteolytic degradation and offer chemodiversity.
  • They mimic peptide primary structures and can be synthesized efficiently.
  • Demonstrated cell membrane permeability (Tat mimic) and specific cell surface targeting (RGD mimic).
  • Exhibited potent antimicrobial activity against drug-resistant pathogens.
  • Inhibited Aβ40 aggregation, indicating potential for Alzheimer's disease intervention.
  • Identified γ-AApeptides that antagonize STAT3/DNA interactions.

Conclusions:

  • γ-AApeptides represent a promising new class of peptidomimetics with diverse biological activities.
  • Their stability, mimicry capabilities, and structural versatility enable broad applications in chemical biology and medicine.
  • Further research into γ-AApeptides could lead to novel therapeutics and diagnostic tools.