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Amino Acids - Anti

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Amino Acids - Anti

Imp for gpat exam. Easily remember gor exam.

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mukul sidhque
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[@: PHARMA eee Se p= SAPIENCE ° Pal on @Bhopal iereny) @Sagar —- @Gwalior @ Kanpur AMINO ACIDS AMINO ACIDS Introduction ‘* Amino acids are a group of organic compounds containing two functional groups— amino and ‘carboxyl. The amino group (—NH2) is basic while the carboxyl group (—COOH) is acidic in nature. Only L- Alpha (a) Amino Acids occurs in Proteins. 20 Amino acids are present in natural protein. 21" Amino acid Seleno-Cysteine & 22" amino acid is pyrrolysine ‘© Proline is the only IMINO ACID. Essential Amino Acids ‘+ The 10 amino acids listed below cannot be synthesized in humans and therefore must be provided from dietary sources. These are called the essential amino acids. ‘© Arginine is required only during periods of growth, or positive nitrogen balance. Arginine Methionine Histidine Phenylalanine Isoleucine Threonine Leucine Tryptophan Lysine Valine Classification ‘Structural classification of L-ot-amino acids found in proteins 1. Amino acids with aliphatic side chains Glycine Gly Alanine Ala Valine val Leucine Leu Isoleucine lle II, Amino acids containing hydroxyl (—OH) groups + Serine ser © Threonine Thr + Tyrosine Tr IIL Sulfur containing amino acids + Gysteine os + Methionine Met IV.Acidic amino acids and their amides Aspartic acid Asp + Asparagine Asn © Glutamic acid Glu © Glutamine Gin V. Basic amino acids © lysine Lys + Arginine ag + Histidine His Branched chain Branched chain Branched chain Hydroxyl Hydroxy Hydroxy Sulfhydryl Thicether B-Carboxyl Amide Y-Carboxyl Amide Apsatone Amino Guanidino Imidazole ob* PHARMA’ = SAPIENCE N Kévcip ofbeit Preime Download Our App from > Google Play Like us on subserbeuson (EB YouTube For more queries visit us at: www.pharmasapience.com [@: PHARMA eee Se p= SAPIENCE ° Pal on @Bhopal iereny) @Sagar —- @Gwalior @ Kanpur VI. Aromatic amino acids © Phenylalanine Phe Benzene or phenyl Tyrosine Tyr Phenol ‘Tryptophan Tp Indole ino acid Proline Pro. Pyrrolidine On the Basis of polarity and solubility —______|a ¥ ¥ Hydrophobic (Nonpolar) Amino acid Hydrophoilic (polar) Amino acid ‘Tryptophane 1) Uncharged (neutral) Tyrosine “Serine - Aspargine Methionine -Theonine - Cysteine Leucine Amino acids may be sweet (Gl, Ala, Val) tasteless (Leu) or bitter (Arg, Ile. > Monosodium glutamate (MSG; ajinomoto) is used as a flavoring agent in food industry, and Chinese foods to increase taste and flavor. soe o) Download Our App ftom >> Google Play 2 eee Like us on subserbeuson (EB YouTube s ‘Group of Best Pharma For more queries visit us at: www.pharmasapience.com [@: PHARMA eee Se p= SAPIENCE ° Pal on @Bhopal iereny) @Sagar —- @Gwalior @ Kanpur } Insome individuals intolerant to MSG, Chinese restaurant syndrome (brief and reversible flulike symptoms) is observed. Optical properties: All the amino acids except glycine possess optical isomers due to the presence of asymmetric carbon atom Photochromicity ~ The Property of Photochromicity i.e. absorbance of UV light (at 250-290 nm) is. seen with aromatic amino acids (Tryptophan, Tyrosine, Phenyl Alanine) ‘Amino acids as ampholytes: > Amino acids contain both acidic (COOH) and basic (NH) groups. > They can donate a proton or accept a proton, hence amino acids are regarded as ampholytes Zwitterion or dipolar ion: > 2witter ion (or dipolar ion) is a hybrid molecule containing positive and negative ionic groups. > The amino acids rarely exist in a neutral form with free carboxylic (COOH) and free amino (NH2) groups. In strongly acidic pH (low pH), the amino acid is positively charged (cation) while in strongly alkaline pH (high pH), it is negatively charged (anion) Each amino acid has a characteristic pH (e.g. leucine, pH 6.0) at which it carries both Positive and negative charges and exists as zwitterions. Isoelectric pH (symbol pl) is defined as the pH at which a molecule exists as a 2witterion or dipolar ion and carries no net charge. Thus, the molecule is electrically neutral EXISTENCE OF AMINO ACID AS CATION,ANION AND ZWITTERION H core YY H as NH. H Amino acid RCcooH, RECO NIE NH Cation Anion ow Ne ae pH) thew A Zwitterion Gsaelvetic: pED) s 1 7 Download Our App ftom >> Google Play < SAPIENCE Like us on subscribe uson (EB YouTube ‘Group of Best Pharma For more queries visit us at: www.pharmasapience.com [@: PHARMA eee Se p= SAPIENCE ° Pal on @Bhopal iereny) @Sagar —- @Gwalior @ Kanpur ‘Amino acids useful as drugs D-Penicillamine (D-dimethyiglycine), a metabolite of penicillin, is employed in the chelation therapy of Wilson’s disease. This is possible since D-penicillamine can effectively chelate copper. N-Acetyleysteine is used in cystic fibrosis, and chronic renal insufficiency, as it can function as an antioxidant. Gabapentin (Y-aminobutyrate linked to cyclohexane) is used as an anticonvulsant, A selected list of important non-protein amino acids along with their functions ino acids Function |. a-Amino acids Ornithine Citralline > Intermediates in the biosynthesis of urea Arginosuccinic acid Thyroxine —— Triiodothyronine Thyroid hormones derived from tyrosine. S-Adenosylmethionine -Methyl donor in biological system. Homocysteine Intermediate in methionine metabolism. A risk factor for coronary heart diseases Homoserine -Intermediate in threonine, aspartate and methionine metabolisms. 3, 4-Dihydroxy phenylalanine -A neurotransmitter, serves as a precursor for melanin pigment. (D0PA) -Derived from muscle and excreted in urine Creatinine Ovothiol -Sulfur containing amino acid found in fertilized eggs, and acts as an antioxidant ‘Azaserine ‘Anticancer drug Cycloserine -Antituberculosis drug II, Non-a-amino acids B-Alanine -Component of vitamin pantothenic acid and coenzyme A B-Aminoisobutyric acid -End product of pyrimidine metabolism. Y-Aminobutyric acid (GABA) ‘A neurotransmitter produced from glutamic acid 8-Aminolevulinic acid (ALA) -Intermediate in the synthesis of porphyrin (finally heme) Taurine -Found in association with bile acids. Soe © Download Our App ftom >> Google Play re 2 eee Like us on subserbeuson (EB YouTube 2 s Aecare ba Pearse wale: For more queries visit us at: www.pharmasapience.com 1 ®| @ Delhi (South) @ Delhi (East) @ Chandigarh @ Nagpur Pa -P HARMA NCE @ Raipur @indore — @PBhopal weneee) @ Bhopal i) @Bhopal iereny) @Sagar —- @Gwalior @ Kanpur ‘Amino acids and their derivatives as neurotransmitters Amino acid/derivative Major Function(s) Glycine Inhibitory neurotransmitter in spinal cord Glutamate Excitatory neurotransmitter Dopamine Increases blood pressure Hormonal neurotransmitters, increase cardiac output & blood pressure Serotonin Regulates cerebral activity and behavior Gamma-Aminobutyric acid (GABA) Inhibitory neurotransmitter in brain Norepinephrine and epinephrine ‘Amino acid i Function(s) Serine Ethanolamine Forms choline Glutamate Gamma-Aminobutyric acid Inhibitory neurotransmitter Histidine Histamine Vasodilator, promotes gastric HCI & pepsin synthesis Phenylalanine Dopamine For the synthesis of norepinephrine & epinephrine 2 Tyrosine Tyramine Vasoconstrictor (increases blood pressure) ‘Tryptophan Tryptamine Elevates blood pressure Serotonin Stimulates Cerebral activity Melatonin Circadian rhythms 1 2 3 4. 5. 6 7. 8 9 Cysteine Taurine Constituent of bile acid (taurocholic acid) Products formed/contributed by amino acids No. | Amino acid Specialized product(s) Glycine Creatine, glutathione, heme, purines, conjugated bile acids Tyrosine Thyroxine, triiodothyronine, epinephrine, norepinephrine, dopamine, melanin Tryptophan NAD+, NADP+ (coenzymes of niacin), serotonin, melatonin. Methionine Active methionine, creatine, epinephrine, polyamines cysteine Glutathione, taurine, coenzyme A, active sulfate. Histidine Histamine Arginine Creatine, nitric oxide Lysine Carnitine Glutamate Gamma-Amino butyric acid, glutathione, Gamma-carboxyglutamate Glutamine Purines, pyrimidines, amino sugars Aspartate Purines, pyrimidines Serine Phosphatidylserine, sphingomyelins, choline. beta-Alanine Coenzyme A Soe © Download Our App ftom >> Google Play re 2 eee Like us on subserbeuson (EB YouTube 2 s ‘Group of Best Pharma Breins For more queries visit us at: www.pharmasapience.com [@: PHARMA eee Se p= SAPIENCE ° Pal on @Bhopal iereny) @Sagar —- @Gwalior @ Kanpur ‘TRANSAMINATION The transfer of an amino (NH2) group from an amino acid to a keto acid is known as transamination, This process involves the interconversion of a pair of amino acids and a pair of keto acids Itis catalysed by a group of enzymes called transaminases or aminotransferase Salient features of transamination © All transaminases require pyridoxal phosphate (PLP), a coenzyme derived from vitamin B6. © Specific transaminases exist for each pair of amino and keto acids. © However, only two— namely, aspartate transaminase and alanine transaminase—make a significant contribution for transamination. ‘There is no free NH3 liberated, only the transfer of amino group occurs. Transamination is reversible A Amino acid, ae-Keto acid acketo acid,” PLP ino acids vie © Download Our App ftom >> Google Play = Ss ENCE Like us on subscribe us on YouTube LD Aércipafieit Prairie For more queries visit us at: www.pharmasapience.com al ®] @ Delhi (South) @ Delhi (East) @Chandigarh — @ Nagpur e ARMA P = @raipur @indore — @Bhopal (wenses1 @ Bhopal = SAPIENCE @Bhopal iereny) @Sagar —- @Gwalior @ Kanpur PEPTIDES The amino acids are held together in a protein by covalent peptide bonds or linkages. These bonds are rather strong and serve as the cementing material between the individual amino acids (considered as bricks). > Formation of a peptide bond: © When the amino group of an amino acid combines with the carboxyl group of another amino acid, a peptide bond is formed. Note that a dipeptide will have two amino acids and one peptide (not two} bond. Peptides containing more than 10 amino acids (decapeptide) are referred to as polypeptides. | H Peptide Bond Merrifield synthesis: ©The established method for the production of synthetic peptides in the lab is known as Solid-Phase Peptide Synthesis (SPPS). © Pioneered by Robert Bruce Merrifield, SPPS allows the rapid assembly of a peptide chain ‘through successive reactions of amino acid derivatives on an insoluble porous support. Characteristics of peptide bond: ©The peptide bond is rigid and planar with partial double bond in character. ©. Itgenerally exists in trans configuration. © Both COand NH groups of peptide bonds are polar and are involved in hydrogen bond formation. Writing of peptide structures: © Conventionally, the peptide chains are written with the free amino end (N-terminal residue) at the left, and the free carboxyl end (C-terminal residue) at the right. © The amino acid sequence is read from N-terminal end to C-terminal end. © Incidentally, the protein biosynthesis also starts from the N-terminal amino acid, soe o) Download Our App ftom >> Google Play < SAPIENCE Like us on subscribe uson (EB YouTube ‘Group of Best Pharma For more queries visit us at: www.pharmasapience.com SQ: PHARMA me come Se p= SAPIENCE |2™" riven @ span @Bhopal iereny) @Sagar —- @Gwalior @ Kanpur > Shorthand to read peptides: © Theamino acids in a peptide or protein are represented by the 3-letter or one letter abbreviation. © Thisis the chemical shorthand to write proteins. > Naming of peptides: © Fornaming peptides, the amino acid suffixes -ine (glycine), an (tryptophan), -ate (glutamate) are changed to -yl with the exception of C-terminal amino acid. © Thus a tripeptide composed of an N terminal glutamate, a cysteine and a C-terminal glycine is called glutamyl-cysteinyl-glycine. Determination of amino acid sequence: ‘The polypeptides or their smaller fragments are conveniently utilized for the determination of sequence of amino acids. This is done in a stepwise manner to finally build up the order of amino acids in a protein. Certain reagents are employed for sequence determination > N-terminal degradation © Sanger’s reagent: Sanger used 1-fluoro 2,4-dinitrobenzene (FDNB) to determine insulin structure. FDNB specifically binds with N-terminal amino acid to form a dinitrophenyl (DNP) derivative of peptide. This on hydrolysis yields DNP-amino acid (N-terminal) and free amino acids from the rest of the peptide chain. Edman’s reagent : Phenyl isothiocyanate is the Edman's reagent. It reacts with the Nterminal amino acid of peptide to form a phenyl thiocarbamyl derivative, Dansyl method (1-dimethyl amino naphthalene-5- sulphony! chloride) Sequenator : This is an automatic machine to determine the amino acid sequence in a polypeptide (with around 100 residues). It is based on the principle of Edman’s degradation (described above). Amino acids are determined sequentially from N-terminal end. terminal degradation ‘Schlack and kumpf method- In this method the amino group is first protected by benzoylation and then the C-terminal amino acid is converted into thio hydantoin which is hydrolysed Ultimately to the amino acid exactly in the same manner as in Edman method- Reductive method-The method is based on the fact that the lithium aluminum hydride or lithium borohydride reduces the free terminat carboxyl group of the peptide to a primary alcoholic group. Hydrazinolysis:-The peptide (or protein) is heated with anhydrous hydrazine at 100°C which converts all of the amino acids ( except the3 carboxyl terminal one) of the chain into amino acid hydrazides. Soe © Download Our App ftom >> Google Play re 2 eee Like us on subserbeuson (EB YouTube 2 s Fema a eC PRT RCIA For more queries visit us at: www.pharmasapience.com

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