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Related Concept Videos

Protein Digestion01:02

Protein Digestion

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Protein digestion begins in the stomach, where the highly acidic environment can easily disrupt protein structure by exposing the peptide bonds of polypeptide chains. After polypeptide chains are broken into individual amino acids by a series of digestive enzymes, the amino acids are transported to the liver via the bloodstream to produce energy.
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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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Peptide Identification Using Tandem Mass Spectrometry01:33

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Tandem mass spectrometry, also known as MS/MS or MS2, is an analytical technique that employs two mass analyzers. Essentially it is a series of mass spectrometers that helps isolate a particular biomolecule and then helps study its chemical properties.
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Proteins are the building block of life. They are also  the most abundant macromolecules with as many diverse roles in the body. They are part of many structural components that provide unique shapes and structures to animal cells, tissues, and organs. In addition, they also act as biological catalysts and carry out several anabolic and catabolic reactions. Notably, some proteins are chemical messengers and regulate many critical processes, such as metabolism, growth, and development. They...
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Transducer Mechanism: Enzyme-Linked Receptors01:27

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Enzyme-linked receptors are cell-surface receptors acting as an enzyme or associating with an enzyme intracellularly. They make excellent drug targets. Drugs can bind to the extracellular ligand-binding domain or directly affect their enzymatic domain and alter their activity.
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The Proteasome Structure01:17

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The ubiquitin-proteasome pathway is a well-known mechanism utilized by eukaryotic cells to remove cytoplasmic proteins that are misfolded, damaged, or no longer needed. In this pathway, the protein that needs to be eliminated undergoes a process called ubiquitination, where a chain of ubiquitin molecules is attached to the 48th lysine residue of the target protein. This ubiquitin modification helps the proteasome distinguish between a target protein and a healthy protein.
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Peptides from Phage Display Library Modulate Gene Expression in Mesenchymal Cells and Potentiate Osteogenesis in Unicortical Bone Defects
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Bioactive peptides.

Fereidoon Shahidi1, Ying Zhong

  • 1Memorial University of Newfoundland, Department of Biochemistry, 300 Prince Philip Dr, St. John's, NL, Canada. fshahidi@mun.ca

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|August 30, 2008
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Summary
This summary is machine-generated.

Bioactive peptides from food sources offer health benefits and can be used as functional ingredients. Research is ongoing to explore their sources, effects, and preparation methods for health promotion.

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Area of Science:

  • Biochemistry and Food Science
  • Nutritional Science
  • Pharmacology

Background:

  • Food-derived peptides generated during digestion or processing exhibit significant biological activities.
  • These bioactive peptides play a crucial role in metabolic regulation and modulation.
  • Their properties suggest potential applications as nutraceuticals and functional food ingredients for enhancing health and reducing disease risk.

Purpose of the Study:

  • To review the diverse bioactivities of peptides derived from various food sources.
  • To highlight the ongoing research into the sources, bioavailability, and mechanisms of action of these peptides.
  • To discuss technological advancements in the preparation, purification, and characterization of bioactive peptides.

Main Methods:

  • Literature review of studies on food-derived bioactive peptides.
  • Analysis of reported bioactivities, including antihypertensive, antioxidant, and immunomodulatory effects.
  • Examination of research on peptide sources, bioavailability, and technological preparation methods.

Main Results:

  • Numerous studies confirm a wide range of bioactivities for food-derived peptides.
  • Identified activities include antihypertensive, antioxidant, anticancer, antimicrobial, opioid, immunomodulatory, and cholesterol-lowering effects.
  • Ongoing research focuses on understanding their physiological roles and optimizing their production.

Conclusions:

  • Bioactive peptides represent a promising area for developing functional foods and nutraceuticals.
  • Further research is essential to fully elucidate their health benefits and mechanisms.
  • Technological innovations are key to harnessing the full potential of these compounds for health promotion.