Presentation on the amino acid glutamic acid. The use of amino acids as medicines. aminopropanoic acid
Amino acids Completed by student 10 a MBOU Secondary School No. 102, Samara Slipkus Vitalia
Plan 1. Physical properties 2. Chemical properties 3. Preparation 4. Optical isomerism 5. Classification 6. Significance
Physical properties a Amino acids are colorless crystalline substances, highly soluble in water and slightly soluble in organic solvents. Many of them have a sweet taste. They have high densities and exceptionally high melting (often decomposition) temperatures.
Chemical properties All amino acids are amphoteric compounds; they can exhibit both acidic properties due to the presence of a carboxyl group in their molecules - COOH, and basic properties due to the amino group - NH 2. Solutions of amino acids in water have the properties of buffer solutions, i.e. are in a state of internal salts. Amino acids can usually undergo all the reactions characteristic of carboxylic acids and amines. An important feature of amino acids is their ability to polycondensate (the process of polymer synthesis), leading to the formation of polyamides, including peptides, proteins, nylon, and nylon.
Obtaining Most amino acids can be obtained through protein hydrolysis or as a result of chemical reactions:
Optical isomerism All α-amino acids found in living organisms, except glycine, contain an asymmetric carbon atom (threonine and isoleucine contain two asymmetric atoms) and have optical activity. Almost all naturally occurring α-amino acids are L-form, and only L-amino acids are included in proteins synthesized on ribosomes.
Classification Nonessential amino acids are amino acids that can enter our body with protein foods or be formed in the body from other amino acids. Essential amino acids are those amino acids that our body cannot produce on its own; they must be supplied with protein foods.
Significance Amino acids are the main “building material” for the synthesis of specific tissue proteins, enzymes, peptide hormones and other physiologically active compounds. In addition to the fact that amino acids form proteins, some of them: Act as neurotransmitters or are their precursors. Neurotransmitters are chemicals that transmit nerve impulses from one nerve cell to another. Thus, some amino acids are essential for normal brain function. Amino acids ensure that vitamins and minerals adequately perform their functions. Some amino acids directly provide energy to muscle tissue.
(aminocarboxylic acids), organic compounds whose molecule simultaneously contains carboxyl and amine groups. They act as monomers in the construction of protein molecules. Colorless crystalline substances, soluble in water. Many have a sweet taste. Only 20 amino acids are involved in protein synthesis.
Classification options
amino acids:
Depending on the position of the amino group
(alpha amino acids, beta amino acids)
According to the configuration of the molecule, there are L and D isomers.
According to optical activity in relation to the plane of polarization.
By participation in protein synthesis (proteinogenic and non-proteinogenic).
According to the structure of the side radical.
According to acid-base properties.
As necessary for the body (replaceable, irreplaceable)
All proteinogenic amino acids are alpha amino acids.
Classification of amino acids (by side radical):
Essential: leucine (LEU, L),
isoleucine (ILE, J), valine (VAL, V), phenylalanine (PEN, F), tryptophan (TRI, W), threonine (TRE, T), lysine (LYS,
methionine (MET,M).
Replaceable ones include:
amino acids whose carbon skeleton
is formed in metabolic reactions and is capable of receiving an amino group to form an amino acid.
Conditionally replaceable. Their synthesis is underway, not in
sufficient quantity, especially in children.
Individual representatives of amino acids and their properties.
Aliphatic:
Glycine (GLY), or glycocol, aminoacetic acid. The only one that is optically inactive. Participates in protein synthesis. Its atoms are part of nucleotides, heme and the tripeptide glutathione.
Alanine (ALA), aminocaproic acid. Used for glucose synthesis.
Valine (VAL), leucine (LEU), isoleucine (ILE) - play an important role in the formation of protein molecules due to their pronounced hydrophobic properties.
Methionine (MET) - performs mobile donor function
methyl group required
The -OH group easily interacts with phosphoric acid, which is sometimes necessary to change the functional activity of proteins. Serine (SER),
threonine (TPE).
Dicarboxylic (containing an additional –COOH group)
Glutamic (GLU), aspartic (ASP). Thanks -COOH these acids promote ionic interaction, impart charge to the protein molecule, and can form amides.
Amides of dicarboxylic acids– glutamine (GLY), asparagine (ASN), lysine (LYS), arginine (ARG) - are involved in the neutralization and transport of ammonia.
Cyclic ones have a ring in their radical.
Phenylalanine (PEN), tyrosine (TYR) - involved in the formation of adrenaline and thyroxine. Tryptophan (TRI) - used for the synthesis of vitamin PP, serotornine, pineal gland hormones. Histidine (HIS) - participates in the formation of histamine, which regulates capillary permeability, manifests its effect in allergies.
Separately considered
proline (PRO)
Does not correspond to the general amino acid formula. Part of the collagen structure.
Amino acids included in the composition
proteins exhibit special properties
All are α-amino acids
They are L-stereoisomers
Refers to amphoteric compounds
CLASSIFICATION OF AMINO ACIDS according to the structure of the carbon chain
CLASSIFICATIONAMINO ACIDS by structure
carbon chain
Amino acids
Acyclic (non-cyclic)
Aromatic
Cyclic
Heterocyclic Acid-base classification
groups, the presence of others
functional groups and radicals
Monoaminocarboxylic (neutral)
amino acids:
1) H2N - CH2 - COOH
Aminoacetic acid, 2-aminoethanoic acid,
glycine (GLY)
Sweet in taste, widely distributed in plants
world, is part of albumin, is used as
sedative for nervous disorders *
2) CH3 - CH - COOH
NH2
α-aminopropionic acid, 2-aminopropanoic acid
acid, alanine (ALA)
Source of energy for the brain and central nervous system,
strengthens the immune system, participates in
sugar metabolism *
3) CH2 - CH - COOH
OH
NH2
α-amino-β-hydroxypropionic acid, 2-amino3-hydroxypropanoic acid, serine (SEP)
Included in plant and animal proteins
origin, there is a lot of casein in milk,
refers to hydroxyamino acids *
4) CH2 - CH - COOH
SH
NH2
α-amino-β-thiopropionic acid,
2-amino-3-mercaptopropanoic acid,
cysteine (CIS)
Participates in the exchange of sulfur in the body, has
radioprotective effect, metabolic disorder
cysteine leads to changes in the lens of the eye and
cataract
٭٭CH2 - CH - COOH
2
S
CH2 - CH - COOH
-2H
SH
+2H
NH2
S
NH2
NH2
CH2 - CH - COOH
2-amino-3propanoic acid disulfide,
cystine (CY-S-S-CY)
Cystine is the only diamino-dicarboxylic
amino acid *
5) CH2 - CH2 - CH - COOH
S-CH3
NH2
α-amino-γ-methylthiobutyric acid,
2-amino-4-methylthiobutanoic acid,
methionine (MET)
Methionine has a methyl group due to which
helps prevent fatty liver,
participates in the synthesis of hormones, enzymes, due to
mobile methyl group is capable of removing
toxic substances. Methionine is used in
as a medicinal product for the treatment and
liver disease prevention Methionine, cysteine and cystine
classified as sulfur-containing
amino acids, especially
a lot in proteins that are included
in the composition of horny formations:
hair, wool, horns, hooves,
nails *
6) CH3 -CH - CH - COOH
CH3NH2
α-aminoisovaleric acid,
2-amino-3-methylbutanoic acid,
valine (VAL)
One of the main components of tissue growth,
used as an antidepressant *
*
7) CH3 -CH - CH - COOH
OH
NH2
α-amino-β-hydroxybutyric acid,
2-amino-3-hydroxybutanoic acid,
threonine (TPE)
It has lipotrophic properties and is necessary for
synthesis of immunoglobulins and antibodies, important
component of collagen, elastin and enamel protein *
8) CH3 -CH -CH2 - CH - COOH
CH 3
NH2
α-aminoisocaproic acid,
2-amino-4-methylpentanoic acid,
leucine (LEU)
Leucine in large quantities
found in hemoglobin, casein,
egg albumin, lowers
blood sugar levels, contributes to
wound healing, absent in
alcoholics and drug addicts *
*
9) CH3 -CH2 -CH - CH - COOH
CH3 NH2
α-amino-β-methylvaleric acid,
2-amino-3-methylpentanoic acid,
isoleucine (ILE) Monoaminodicarbonic
amino acids:
(sour)
*
10) HOOC -CH2 - CH - COOH
NH2
α-aminosuccinic acid,
2-aminobutadioic acid,
aspartic acid (ASP)
Takes part in transamination reactions, in
the functioning of the immune system and the synthesis of nucleic acids
acids Monoaminodicarbonic
(acidic) amino acids:
*
11) HOOC -CH2 - CH2 - CH - COOH
NH2
α-aminoglutaric acid,
2-aminopentanedioic acid,
glutamic acid (GLU)
Source of amino group in metabolic
processes O
*
C -CH2 - CH - COOH
H2N
NH2
Aspartic acid amide (ASH) O
H2N
*
C -CH2 - CH2 - CH - COOH
NH2
Glutamic acid amide (GLN)
There is more glutamine in the body than others
amino acids, it is necessary for the synthesis of glycogen and
energy exchange in muscle cells, improves
short-term and long-term memory Diaminomonocarboxylic acids
(basic) amino acids:
*
12) H2N - CH2 - CH2 - CH2- CH2 - CH - COOH
NH2
α,ε-diaminocaproic acid,
2,6-diaminohexanoic acid,
lysine (LYS)
Provides calcium absorption, participates in
collagen formation, production of antibodies, hormones,
enzymes Diaminomonocarboxylic acids
(basic) amino acids:
*
13) H2N - C - NH - CH2 - CH2- CH2 - CH - COOH
N.H.
NH2
α-amino-Δ-guanidyl valeric acid,
2-amino-5-guanidylpentanoic acid,
arginine (ARG)
Causes a slowdown in the development of tumors, strengthens
immune system, promotes muscle growth
masses Aromatic amino acids
*
14)
CH2 - CH - COOH
NH2
α-amino-β-phenylpropionic acid,
2-amino-3-phenylpropanoic acid,
phenylalanine (PEN)
Necessary for the synthesis of tyrosine and hormones,
regulates the functioning of the thyroid gland,
helps regulate the natural color of the skin,
through the formation of melanin pigment Aromatic amino acids
*
CH2 - CH - COOH
15)
HO
NH2
α-amino-β-(n-hydroxyphenyl)-propionic acid,
2-amino-3-(4-hydroxyphenyl)-propanoic acid,
tyrosine (TYR)
Necessary for normal functioning of the adrenal glands,
thyroid gland and pituitary gland, has a powerful
stimulating effect
N
16)
*
CH2 - CH - COOH
N
H
NH2
α-amino-β-imidazolylpropionic acid,
2-amino-3-imidazolylpropanoic acid,
histidine (HIS)
Plays an important role in protein metabolism and synthesis
hemoglobin is one of the most important regulators
blood clotting Heterocyclic amino acids:
*
CH2 -CH - COOH
17)
NH2
N
H
α-amino-β-indolylpropionic acid,
2-amino-3-indolylpropanoic acid,
tryptophan (TRI)
Natural relaxant, helps fight
state of anxiety and insomnia Imino acids:
18)
*
COOH
N
H
Pyrrolidine-2-carboxylic acid,
proline (PRO) Imino acids:
OH
*
19)
*
COOH
N
H
4-hydroxypyrrolidine-2-carboxylic acid,
hydroxyproline (HO-PRO) Classification of amino acids depending on the radical
Non-polar (hydrophobic)
Polar(hydrophilic)
POLAR AMINO ACIDS
IONOGENICNONIONIC
CAPABLE OF DISSOCIATION
IN THE CONDITIONS OF THE ORGANISM
CH2 - CH - COOH
HO
NH2
tyrosine
UNABLE
HO - CH2 - CH - COOH
NH2
serine Polar amino acids with
ionogenic groups under conditions
organisms can be in the form
anions and cations
In the form of anions
In the form of cations
Asp
Liz
Glu
Arg
Shooting gallery
Gies
Cis Polar ionogenic
radicals are located
both on the surface and
inside protein molecules.
They participate in
formation of hydrogen
connections with others
polar groups All α-amino acids except
glycine, have an asymmetric atom
carbon and exist in the form
enantiomers belonging to the D- and L-series. In animal proteins
L-amino acids are present in proteins
microorganisms are found and
D-series amino acids. D-amino acids
are not absorbed by the animal body STEREOISOMERISM OF α-AMINO ACIDS
COOH
H2N
COOH
H
H2N
H
CH3
L-alanine
CH3
L-threonine
COOH
H
H2N
H
OH
H3C
H
C2H5
L-isoleucine Three amino acids have two
center of chirality
threonine
isoleucine,
4-hydroxyproline 15.2. BIOSYNTHETIC PATHWAYS
AMINO ACIDS FORMATION
Biosynthesis of α-amino acids
carried out from α-keto acids of carbohydrate metabolism products.
There are two possible ways of transformation
keto acids to amino acids 1) Reductive amination
with the participation of coenzyme NAD-H
HOOC-CH2-CH2-C-COOH
O
+NH3
HAD-H
α-ketoglutaric acid
HOOC-CH2-CH2-CH-COOH
NH2
glutamic acid 2) Transamination (transamination)
the source of the NH2 group for keto acids is
other amino acid
pyridoxal phosphate
R-CH-COOH
NH2
+
HOOC-CH2-C-COOH
O
Oxaloacetic acid
HOOC-CH 2-CH-COOH
NH2
Aspartic acid 15.3. CHEMICAL PROPERTIES
Amino acids are amphoteric compounds, in
solutions exist in the form of bipolar
ions
H3+N – CH – COOR Amino acids have all the properties of
carboxylic acids and amines
Reactions of carboxyl group formation of functional
acid derivatives (esters,
amides, salts, acid halides).
Reactions of the amino group - formation of salts
with strong acids, formation of Nacylated derivatives Characteristic of amino acids
a number of specific
reactions caused
presence in their structure
COOH- and NH2- groups in
the same atom
carbon 1) Decarboxylation in vivo
leads to the formation of biogenic
amines
1)
HOOC-CH2-CH2-CH-COOH
→ HOOC-CH2- CH2-CH2- NH2
GLU
│
- CO2 γ-aminobutyric acid
NH2
natural tranquilizer
in vitro
t0C, Ba(OH)2
HOOC-CH2-CH2-CH-COOH
→
│
- BaCO3
NH2
HOOC-CH2-CH2-CH2-NH2 As a result of the reaction
decarboxylation
biogenic amines are formed
(tryptamine, histamine,
colamine, dopamine, serotonin) 2) Deamination (removal of NH2 group)
a) direct deamination in vivo
H
HOOC -CH2 -CH -COOH
Aspartase
COOH
C=C
-NH3
NH2
Aspartic acid
HOOC
H
Fumaric acid b) Oxidative deamination in vivo
occurs with the participation of the coenzyme NAD+
+
+ OVER
R-CH-COOH
R - C - COOH
R - C - COOH
-NH3
-OVER-N
NH2
H2O
N.H.
O Deamination in vitro
CH3 - CH - COOH
CH3 - CH - COOH
+
HNO2
NH2
Method
+ N2
+ H2O
OH
Van Slyke,
it is applied for
amino acid quantification 3) hydroxylation
amino acids, has no analogy
in in vitro chemistry
phenylalanine
hydroxylase a
CH2 - CH - COOH
HO
CH2 - CH - COOH
NH2
NH2
HAIRDRYER
TIR
Absence or deficiency in the body
enzyme that catalyzes this reaction
leads to severe disease phenylketonuria
(proteios, Greek - first) Proteins (proteins, polypeptides) high-molecular organic substances consisting of α-amino acids connected in a chain by a peptide bond. In living organisms, the amino acid composition of proteins is determined by the genetic code. α-Amino acids - monomers for protein synthesis More than 300 amino acids have been found in nature, but only 20 (α-amino acids) are found in proteins.
Classification of amino acids Carboxyl group Radical Amino group Amino acids (aminocarboxylic acids) are organic compounds whose molecule simultaneously contains a carboxyl and an amino group of the 2-aminoethanoic acid group - aminoacetic acid glycine 2 or α 3-aminobutanoic acid - aminobutyric acid 1. Structural classification 1.1. Mutual arrangement of COO- and NH groups Nature of radical (R): aliphatic, aromatic, heterocyclic leucine anthranilic acid histidine 1.3. Number of COO- and NH 2 - groups: monoaminocarboxylic, monoaminodicarboxylic, diaminocarboxylic glycine aspartic acid lysine
Proteinogenic amino acids (“giving birth to proteins”) are natural amino acids involved in the construction of peptide and protein molecules Alanine (Ala) Valine (Val) Leucine (Leu) Isoleucine (Ile) Arginine (Arg) Lysine (Lys) Threonine (Tre) (Methionine ( Met) Phenylalanine (Phe) Tryptophan (Try) Essential amino acids Histidine (His)
Configuration of proteinogenic amino acids Configuration is the arrangement of atoms that characterizes a particular stereoisomer (+) -Alanine (-) -Alanine? L-amino acid L – glyceraldehyde R,S – nomenclature L,D – nomenclature L,D – nomenclature used for amino acids and carbohydrates R,S – nomenclature (see R. Morrison, R. Boyd. Organic chemistry, p. 87)
Acid-base properties of amino acids Bipolar ions, zwitterions High melting point. (WITH); soluble in water; insoluble in non-polar organic solvents. Amino acids are amphoteric compounds. Isoelectric point is the pH value of the environment at which the amino acid exists predominantly in the form of a zwitterion.
Proteins Primary structure - sequence of amino acids in a polypeptide chain Secondary structure - local ordering of a fragment of a polypeptide chain, stabilized by hydrogen bonds Tertiary structure - spatial structure of a polypeptide chain (covalent, ionic bonds, hydrophilic-hydrophobic interactions) Quaternary structure - mutual arrangement of several polypeptide chains as part of a single protein complex
Three-dimensional structure of the hemoglobin molecule. Soluble in water or aqueous solutions of acids, bases, salts. Globular proteins include enzymes, immunoglobulins, transport and regulatory hormones, antibodies, egg albumin, hemoglobin, fibrinogen, fibrin Globular proteins - polypeptide chains are tightly folded into compact spherical structures (globules) Fibrillar proteins - polypeptide chains having an elongated thread-like structure Insoluble in water. Fibrillar proteins include α-keratins, collagen, fibroin.
Amines are organic compounds that are derivatives of ammonia, in the molecule of which one, two or three hydrogen atoms are replaced by hydrocarbon radicals. According to the number of substituted hydrogen atoms, primary, (one hydrogen atom is substituted), secondary (two of three hydrogen atoms are substituted) and tertiary (three of three hydrogen atoms are substituted) amines are distinguished, respectively.
Sulfonamide preparations (sulfonamides) - these include derivatives of sulfanilic acid, in finished form they are white or slightly yellowish odorless and tasteless powders, poorly soluble in water. Their antimicrobial effect is mainly due to the fact that they disrupt the process of microbes obtaining the “growth” factors necessary for their life and development - folic acid and other substances. Taking sulfonamides in insufficient doses or stopping treatment too early can lead to the emergence of resistant strains of pathogens that are not susceptible to further action of sulfonamides.
Quinoline Derivatives of quinoline are used in medicine (plasmocide, quinine). plasmacidquinine Quinine - has antipyretic and analgesic properties, as well as a pronounced effect against malarial plasmodia. Plasmocid synthetic antimalarial drug
A MINO ACIDS Amino acids (aminocarboxylic acids) are organic compounds whose molecule simultaneously contains carboxyl and amine groups. Amino acids can be considered as derivatives of carboxylic acids in which one or more hydrogen atoms are replaced by amine groups.
APPLICATION IN MEDICINE. Amino acids are widely used in modern pharmacology. Being not only structural elements of proteins and other endogenous compounds, they are of great functional importance. Some of them act as neurotransmitter substances. Some amino acids have found independent use as medicines.
Amino acids are also used as parenteral nutrition for patients, that is, bypassing the gastrointestinal tract, with diseases of the digestive and other organs; and also for the treatment of liver diseases, anemia, burns (methionine), stomach ulcers (histidine), and neuropsychiatric diseases (glutamic acid, etc.). Amino acids are used in animal husbandry and veterinary medicine for the nutrition and treatment of animals, as well as in the microbiological, medical and food industries.
It is important to take amino acids with cofactors, which are usually vitamins, mineral salts or other nutrients that help amino acids through metabolic processes in the human body. It is also important to take amino acids as a whole, rather than just one amino acid, because amino acids involve complex metabolic pathways that require different cofactors and other amino acids.
LITERATURE 1) iy-tip-okisleniya.html 2) T.T. Berezov Biological chemistry 3) B.F. Korovkin Biological chemistry
