CHEMISTRY OF AMINO ACIDS

BY-
MOULI SARKAR
SISTER TUTOR
PRIYAMVADA BIRLA INSTITUTE OF NURSING
 AMINO ACIDS
 Proteins are the basis for the major structural
components of animal and human tissue
Linear chains of amino acids residues .
Amino Acids(AA):
 1 central carbon atom+4 subgroups {amino

group(—NH2),carboxyl group(—COOH),hydrogen
atom,and a distinctive side chain(R)}
 Organic molecules serve as chemical messengers

between cells or function a important intermediates

in metabolic processes.
 Only L-amino acids are in proteins, D-amino acids

are widely in bacterial cell walls.

 300AA in nature but only 20 of these in proteins.

 Not every protein contains all of the 20 AA types.

 MEDICAL AND BIOLOGICAL IMPORTANCE OF
AMINO ACIDS

 1. Amino acids serve as building blocks of proteins. Some amino

acids are found in free form in human blood.
 2. They also serve as precursors of hormones, purines, pyrimidines,
porphyrins, vitamins and biologically important amines like
histamine.
 3. Peptides have many important biological functions. Some of them
are hormones. They are used as anti-biotics and antitumor agents.
 4. Some peptides are required for detoxification reactions. Some
peptides serve as neurotransmitters.
 5. Amino acid proline protects living organisms against free radical
induced damage.
 MEDICAL AND BIOLOGICAL IMPORTANCE
OF AMINO ACIDS CONT..
 6. Some peptides are involved in regulation of cell cycle
and apoptosis.
 7. Peptides of vertebrates and invertebrates act as
antimicrobial agents. They are part of innate immunity.
Bacterial infections at epithelial surface induce
production of antimicrobial peptides, which cause lysis of
microbes.
 8. Peptides are enzyme inhibitors. Natural and synthetic
peptide inhibitors of angiotensin converting enzyme
(ACE) act as a anti hypertensives. Peptide inhibitors of
ACE present in physiological foods, lowers blood pressure
after they are absorbed from intestine. Lisinopril,
Enalapril etc. are synthetic peptide inhibitors of ACE that
are used as drugs in the treatment of hypertension.
 9. Some synthetic peptides are used as enzyme
substrates.
 PROPERTIES OF AMINO ACIDS
Physical Properties

 Amino acids are colorless, crystalline solid.

 All amino acids have a high melting point greater than 200o
 Solubility: They are soluble in water, slightly soluble in
alcohol and dissolve with difficulty in methanol, ethanol,
and propanol. R-group of amino acids and pH of the solvent
play important role in solubility.
 On heating to high temperatures, they decompose.
 All amino acids (except glycine) are optically active.
 Peptide bond formation: Amino acids can connect with
a peptide bond involving their amino and carboxylate
groups. A covalent bond formed between the alpha-amino
group of one amino acid and an alpha-carboxyl group of
other forming -CO-NH-linkage. Peptide bonds are planar
and partially ionic.
 Zwitterionic property
CHEMICAL PROPERTIES OF AMINO ACIDS

A zwitterion is a molecule with functional groups, of which at

least one has a positive and one has a negative electrical
charge. The net charge of the entire molecule is zero. Amino
acids are the best-known examples of zwitterions. They
contain an amine group (basic) and a carboxylic group
(acidic). The -NH2 group is the stronger base, and so it picks
up H+ from the -COOH group to leave a zwitterion. The
(neutral) zwitterion is the usual form amino acids exist in
solution.
 Amphoteric property

Amino acids are amphoteric in nature that is they act as both

acids and base since due to the two amine and carboxylic
group present.
 Ninhydrin test

When 1 ml of Ninhydrin solu­tion is added to a 1 ml protein

solution and heated, the formation of a violet color indicates
the presence of α-amino acids.
 CHEMICAL PROPERTIES OF AMINO ACIDS
CONT..
 Xanthoproteic test
The xanthoproteic test is performed for the detection
of aromatic amino acids (tyrosine, tryptophan, and
phenylalanine) in a protein solution. The nitration of
benzoid radicals present in the amino acid chain
occurs due to reaction with nitric acid, giving the
solution yellow coloration.
 Reaction with Sanger’s reagent

Sanger’s reagent (1-fluoro-2, 4-dinitrobenzene) reacts

with a free amino group in the peptide chain in a
mild alkaline medium under cold conditions.
 Reaction with nitrous acid

Nitrous acid reacts with the amino group to liberate

nitrogen and form the corresponding hydroxyl.
 STRUCTURE OF AMINO ACIDS
 All 20 of the common amino acids are alpha-amino acids.
They contain a carboxyl group, an amino group, and a side
chain (R group), all attached to the α-carbon.
 Exceptions are:

 Glycine, which does not have a side chain. Its α-carbon

contains two hydrogens.

 Proline, in which the nitrogen is part of a ring.

 Thus, each amino acid has an amine group at one end and

an acid group at the other and a distinctive side chain. The

backbone is the same for all amino acids while the side
chain differs from one amino acid to the next.
 All of the 20 amino acids except glycine are of the L-

configuration, as for all but one amino acid the α-carbon is

an asymmetric carbon. Because glycine does not contain
an asymmetric carbon atom, it is not optically active and,
thus, it is neither D nor L.
CLASSIFICATION OF AMINO ACIDS
CLASSIFICATION OF AMINO ACIDS ON THE
BASIS OF R-GROUP
 Nonpolar, Aliphatic amino acids: The R groups in this class of
amino acids are nonpolar and hydrophobic. In side chain it
contains branch of group or hydroxy group(-OH) or sulfer made
disulphide bond.
Glycine, Alanine, Valine, leucine, Isoleucine, Methionine, Proline.
 Aromatic amino acids: Phenylalanine, tyrosine, and

tryptophan, with their aromatic side chains, are relatively

nonpolar (hydrophobic). All can participate in hydrophobic
interactions.
 Polar, Uncharged amino acids: The R groups of these amino

acids are more soluble in water, or more hydrophilic, than those of

the nonpolar amino acids, because they contain functional groups
that form hydrogen bonds with water. This class of amino acids
includes serine, threonine, cysteine, asparagine, and glutamine.
 Acidic amino acids: Amino acids in which R-group is acidic or

negatively charged. Glutamic acid and Aspartic acid

 Basic amino acids: Amino acids in which R-group is basic or

positively charged. Lysine, Arginine, Histidine.

CLASSIFICATION OF AMINO ACIDS ON THE
BASIS OF NUTRITION
Essential amino acids (Nine)
 These amino acids cannot be synthesized in the body and,

therefore, must be present in the diet in order for protein

synthesis to occur.
 These essential amino acids are histidine, isoleucine, leucine,

lysine, methionine, phenylalanine, threonine, tryptophan, and

valine.
Semi-essential amino acids: These are growth promoting
factors since they are not synthesised in sufficient quantity
during growth. They include arginine and histidine. They
become essential in growing children, pregnancy and lactating
women.
Non-essential amino acids
 These amino acids can be synthesized in the body itself and

hence not necessarily need to be acquired through diet.

 Arginine, glutamine, tyrosine, cysteine, glycine, proline, serine,

ornithine, alanine, asparagine, and aspartate.

 CLASSIFICATION OF AMINO ACIDS ON THE
BASIS OF THE METABOLIC FATE
 Glucogenic amino acids: These amino acids serve as
precursors gluconeogenesis for glucose formation. Glycine,
alanine, serine, aspartic acid, asparagine, glutamic acid,
glutamine, proline, valine, methionine, cysteine, histidine,
and arginine.
 Ketogenic amino acids: These amino acids breakdown to
form ketone bodies. Leucine and Lysine.
 Both glucogenic and ketogenic amino acids: These
amino acids breakdown to form precursors for both ketone
bodies and glucose. Isoleucine, Phenylalanine, Tryptophan,
and tyrosine
 FUNCTIONS OF AMINO ACIDS
Amino acids are imperative for sustaining the health of the human
body. They largely promote the:
 Production of hormones

 Structure of muscles

 Human nervous system’s healthy functioning

 The health of vital organs

 Normal cellular structure

 The amino acids are used by various tissues to synthesize proteins

and to produce nitrogen-containing compounds (e.g., purines,

heme, creatine, epinephrine), or they are oxidized to produce
energy.
 The breakdown of both dietary and tissue proteins yields nitrogen-

containing substrates and carbon skeletons.

 The nitrogen-containing substrates are used in the biosynthesis of

purines, pyrimidines, neurotransmitters, hormones, porphyrins, and

nonessential amino acids.
 The carbon skeletons are used as a fuel source in the citric acid

cycle, used for gluconeogenesis, or used in fatty acid synthesis.

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