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Peptides

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What are Peptides?

Peptides are short chains of amino acids. In peptides, two or fifty amino acids get linked by peptide bonds. 

When two consecutive - amino acid molecules get linked together by removal of one water molecule and by formation of covalent between C1 of one - amino acid and N2 of another - amino acid, then this type of covalent bond is called peptide bond. Peptide bond formation is given below –

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Thus, we can say peptides are formed by linking two and fifty amino acids by peptide bonds and removal of water molecules. 

Word peptide has been taken from Greek word peptos , which means ‘digested’. 

Chains of peptides which contain less than ten or fifteen amino acids are called oligopeptides. Dipeptides, tripeptides and tetrapeptides etc. come under the class oligopeptides only. 

Polypeptides are long, unbranched chains of peptides up to approximately 50 amino acids. Peptides are essential for proper functioning of cells. These are also studied under the molecular biology. They come under the class of biological polymers, nucleic acids, oligosaccharides, polysaccharides, and oligomers. 

Although peptides and proteins are the same as both are made up of amino acids, but the peptide chains are shorter than proteins. When a polypeptide contains more than 50 amino acids then it is known as protein. 

All peptides have an N – terminal and C – terminal residue at the ends of the peptide chains. Cyclic peptides are exceptions in this case. N – terminal represents the start of polypeptide and referring to the free amine group. C – terminal represents the end of the polypeptide chain and referring to the free carboxyl group. 

Types or Classes of Peptides 

Peptides have been classified according to their sources and functions. Few of its main classes have been discussed below –

  • Ribosomal Peptides – Ribosomal peptides are subjected to proteolysis. They function in higher organisms as hormones. These are of many types such as antimicrobial peptides, tachykinin peptides, vasoactive intestinal peptides, pancreatic polypeptide etc. 

  • Peptones – They are formed during the proteolysis of milk and meat. They are used for growing fungi, bacteria for various purposes. 

  • Milk Peptides – These are formed by digestion of milk protein. They also formed during fermentation of milk. 

  • Dipeptides – These peptides are formed by linkage of two amino acids by one peptide bond. Example – carnosine, anserine etc. 

  • Tripeptides – These peptides are formed by linkage of three amino acids by two peptide bonds. Example – glutathione, ophthalmic acid etc. 

  • Oligopeptides – These peptides are formed by linkage of more than two and less than 20 amino acids by peptide bonds. Example – netropsin, amanitin etc. 

On the basis of number of amino acids peptides can be of many types such as monopeptide, dipeptide, tripeptide (as discussed above), tetrapeptide, pentapeptide, hexapeptide, heptapeptide, octapeptide, nonapeptide and decapeptide. 

Formation of Peptides 

Peptides are formed by the peptide linkage between amino acids. let us understand the peptide formation by taking an example of dipeptide. For the formation of dipeptide, two amino acids approach each other and form a covalent bond between C1 – carbon of carboxylic acid and N2 – nitrogen atom of amino acid group by removal of the water molecule. One amino acid loses its hydrogen atom and another its hydroxyl group. It is a condensation reaction. The covalent linkage formed between two amino acids is called peptide bond (-CO-NH-) or peptide linkage. Formation of peptide bonds consumes energy. As the water molecule is getting removed, so it is a dehydration synthesis process. 

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Formation of a Dipeptide

When these peptide bonds of peptide break, they release energy. These can be broken down by hydrolysis, but it is a very slow process. Enzymes such as peptidases or proteases can catalyze the process. 

Although peptide and protein both are composed of amino acids and carry out various important functions in cells but differ in their various aspects. Difference between peptide and protein is given below –

Difference Between Peptide and Protein 

S.No.

Peptide 

Protein 

1.

Peptides are short chains of amino acids. 

Proteins are longer chains of amino acids. 

2.

They contain approximately 2 or less than 50 amino acids. 

They contain more than 50 amino acids. 

3.

They are not that well defined in their structure. 

They have a well - defined structure. 

4.

Polypeptide is a class of peptides. 

Protein is formed by joining two or mare polypeptides. 

5.

It plays a key role in the functioning of many molecules and proteins as well. 

It plays a key role as enzyme and structural molecule. 


Functions of Peptides

Peptides are fundamental organic compounds of cells. They carry out various important functions in the cell. In human body, they perform key roles in various biological reactions. Few of its functions are listed below –

  • They are important for muscle building. 

  • GHRP 6 (Growth hormone releasing peptide 6) is useful in the growth of our body. 

  • Neuropeptides are used by neurons to communicate with each other. 

  • Various peptides act as hormones such as peptide hormone.

  • Opioidergic agent is a peptide which functions to directly modulate the opioid neuropeptide systems in the brain. 

  • Copper – peptides are useful for flawless skin and protection against harsh sunny conditions. 

  • Some peptides are used for hunger issues as well.

  • They are used for healing purposes as well. 

  • They are useful in increasing the level of prolactin hormone in females. 

  • They function as antibiotics and prevent the growth of microorganisms. 

  • They work as anticancer agents as well. Although many evidences are not there to support that peptides have an active role as anticancer agents.

  • They play a role of mediator in various reactions.

  • Some peptides work as a transporter. They selectively allow certain molecules to pass through the cell membrane. 

This ends our coverage on the topic “Peptide”. We hope you enjoyed learning and were able to grasp the concepts. We hope after reading this article you will be able to solve problems based on the topic. If you are looking for solutions of NCERT Textbook problems based on this topic, then log on to Vedantu website or download Vedantu Learning App. By doing so, you will be able to access free PDFs of NCERT Solutions as well as Revision notes, Mock Tests and much more.


FAQs on Peptides

1. What exactly is a peptide in the context of Class 12 Chemistry?

In chemistry, a peptide is a short chain of amino acids linked together by covalent chemical bonds called peptide bonds. These are formed when the carboxyl group (-COOH) of one amino acid reacts with the amino group (-NH₂) of another, releasing a molecule of water. Peptides are essentially smaller versions of proteins.

2. How is a peptide bond formed between two amino acids?

A peptide bond is a type of amide bond formed through a condensation reaction. The process involves the removal of a water molecule (H₂O). The carboxyl group (-COOH) of one amino acid loses its hydroxyl (-OH) group, and the amino group (-NH₂) of the other amino acid loses a hydrogen (-H) atom. The resulting bond between the carbonyl carbon of the first amino acid and the nitrogen atom of the second is the peptide bond (-CO-NH-).

3. What is the difference between a peptide and a protein?

The primary difference between a peptide and a protein is their size and structure. Peptides are short chains, typically containing between 2 and 50 amino acids. A chain with more than 50 amino acids is generally called a polypeptide. A protein consists of one or more polypeptides folded into a specific, complex three-dimensional structure that is essential for its biological function.

4. What are the different types of peptides based on the number of amino acid residues?

Peptides are classified based on the number of amino acids they contain. The main types are:

  • Dipeptides: Composed of two amino acids linked by one peptide bond (e.g., Aspartame).
  • Tripeptides: Composed of three amino acids linked by two peptide bonds.
  • Oligopeptides: Chains containing a few (typically 2 to 20) amino acids.
  • Polypeptides: Long, continuous chains of many amino acids (usually more than 50), which are the building blocks of proteins.

5. What is an example of a dipeptide structure relevant to the CBSE syllabus?

A classic example is Glycylalanine (Gly-Ala). It is formed when the amino acid Glycine (Gly) links to Alanine (Ala). The carboxyl group of Glycine reacts with the amino group of Alanine. The resulting structure has a free amino group on the Glycine end (the N-terminus) and a free carboxyl group on the Alanine end (the C-terminus).

6. Why are the 'N-terminus' and 'C-terminus' important in a peptide chain?

The N-terminus (amino-terminus) and C-terminus (carboxyl-terminus) are crucial because they define the directionality of the peptide chain. By convention, a peptide sequence is always written from the N-terminus (left) to the C-terminus (right). This directionality is fundamental to its synthesis in biological systems and is essential for determining its final three-dimensional structure and function, as it dictates how the chain will fold.

7. How does the zwitterionic nature of amino acids influence the properties of a peptide?

Since peptides are made of amino acids, they also exhibit zwitterionic properties. A zwitterion has both a positive and a negative charge on the same molecule. In a peptide, the N-terminus carries a positive charge (-NH₃⁺) and the C-terminus carries a negative charge (-COO⁻) at physiological pH. This charge distribution makes peptides polar and influences their solubility in water and their behavior in an electric field, a property utilized in separation techniques like electrophoresis.

8. What determines the primary structure of a protein?

The primary structure of a protein is determined by the specific sequence in which amino acids are linked together in its polypeptide chain(s). This sequence is not random; it is dictated by genetic information. Even a single change in this sequence can alter the protein's final shape and function, as seen in diseases like sickle-cell anaemia.