Peptides are short chains of amino acids linked by peptide bonds. Typically, peptides contain less than 50 amino acids. Anything longer would be considered a protein. Peptides serve many important biological functions. For example:

  • Neuropeptides act as neurotransmitters and signaling molecules in the nervous system
  • Antimicrobial peptides provide defense against pathogens
  • Oxytocin and vasopressin are peptide hormones that influence social behaviors
  • Insulin is a peptide hormone that regulates blood glucose levels

How are peptides formed?

Peptides form when the carboxyl group of one amino acid forms an amide bond with the amino group of another amino acid. This reaction results in a peptide bond being created, releasing a water molecule.

"The peptide bond is key to the function of peptides and proteins in living organisms"

Key properties of peptides:

  • Short chain of 2 to 50 amino acids
  • Bonded by peptide bonds between amino acids
  • Often adopt defined 3D structures
  • Water-soluble
  • Often have biological activity

What do peptides do?

Due to their small size, peptides can:

  • Bind to receptors and initiate cellular signals
  • Modify or inhibit protein-protein interactions
  • Antimicrobial peptides directly kill pathogens
  • Transport molecules across cell membranes

Some peptides play crucial roles in immune responses, blood clotting, nutrient uptake, and more. There is also great interest in developing peptide-based drugs at clinics like Rebalance Hormone Clinic.

Overall, peptides occupy an important middle ground between small molecules and full-sized proteins. Their versatility enables them to conduct key processes related to cell signaling, defense, and homeostasis. Understanding peptide structure and function may lead to new therapeutic approaches.

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