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Karboksipeptidase dan Analisis Peptida

The document discusses amino acids, peptides, and proteins, detailing their structures, classifications, and synthesis methods. It covers the properties of amino acids, the mechanisms of peptide hydrolysis, and techniques for analyzing peptide sequences. Additionally, it explains the different structural levels of proteins, including primary, secondary, tertiary, and quaternary structures.

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0% found this document useful (0 votes)
7 views31 pages

Karboksipeptidase dan Analisis Peptida

The document discusses amino acids, peptides, and proteins, detailing their structures, classifications, and synthesis methods. It covers the properties of amino acids, the mechanisms of peptide hydrolysis, and techniques for analyzing peptide sequences. Additionally, it explains the different structural levels of proteins, including primary, secondary, tertiary, and quaternary structures.

Uploaded by

Karmila
Copyright
© All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
Available Formats
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ASAM AMINO, PEPTIDA,

DAN PROTEIN

INDAH PURNAMA SARY


PENDAHULUAN

 Protein → polimer alami yang terdiri dari


sejumlah unit asam amino yang berikatan amida
(peptida) satu sama lainnya
 Asam amino → monomer protein
 Peptida → oligomer dari asam amino
 Telur, rambut, jaring labah, hemoglobin
ASAM AMINO
ASAM AMINO
 Struktur umum :
dipolar
 Asam amino α
 Amfoterik :
ion zwitter
Jenis Asam Amino
O

 Non Polar netral H2N CH C OH


 Polar netral O


CH2
Polar Asam H2N CH C OH


CH2
Polar Basa CH2
lisina
C O
CH2

O OH
CH2 asam glutamat
H2N CH C OH CH2
O
CH CH3 NH2
H2N CH C OH
CH3
valina CH2
serina
OH
Latihan
 Sebutkan jenis asam amino berikut berdasarkan
kepolarannya !
CO2-
S CO2- CO2-

NH3+
NH3+ NH2+
Methione
(Met; M) Phenylalanine Proline
(Phe; F) (Pro; P)

CO2- CO2-
HO

NH3+ NH3+
Serine Threonine
(Ser; S) (Thr; T)
 Sebutkan jenis asam amino berikut berdasarkan
keasamannya !
CO2-
CO2-
HS

NH3+
NH3+
Cysteine HO
(Cys; C) Tyrosine
(Tyr; Y)

CO2-
N +
H3N CO2-
NH3+
N
H NH3+
Lysine
Histadine (Lys; K)
(His; H)
pH Isoelektrik
 At some intermediate pH called the pI (isoelectric point),
the concentration of the dipolar ion is at a maximum and
the concentrations of anionic and cationic forms are
equal
Sintesis Asam Amino

 Dari -Halo Carboxylic Acids


 Melalui Strecker Reaction
 Gabriel synthesis
 Hidrolisis protein  dalam sistem
kehidupan
 -Halo Carboxylic Acids
O O
H2O
– +
CH3CHCOH + 2NH3 CH3CHCO NH4Br

Br +NH3

 Strecker Reaction
O H2 N CN
C NH3 HCN C
H R H R
-aminonitrile

Heat H3O+, H2O

H3N COO
C
H R
Mekanisme reaksi Strecker Reaction
Gabriel Synthesis
Reaksi pada Asam Amino

Asilasi Esterifikasi
O O
+ –
CH3COCCH3 + H3NCH2COO + CH3CH2OH

HCl

O
O O +

Cl H3NCH2COCH2CH3
CH3CNHCH2COH
Peptida
Hidrolisis Peptida
 Hidrolisis asam  memutus semua ikatan peptida
 Hidrolisis Enzimatis  memutus ikatan peptida tertentu 
menghasilkan fragmen yang bisa dipisahkan dan diidentifikasi
 Enzim yang mengkatalisis pemecahan ikatan peptida adalah
protease, peptidase, dan enzim proteolitik
 Enzim yang spesifik memotong ikatan peptida pada ujung-C :
 Trypsin  lysine dan arginine (lys dan arg)
 Chymotrypsin  Phenilalanine, tyrosine, tryptophan (phe, tyr,
trp)
 Carboxipeptidase  Ujung-C terminal
 Sianogen bromida  methionin (met)
 Enzim yang spesifik memotong ikatan peptida pada ujung-N :
 Pepsin  Phenilalanine, tyrosine, tryptophan (phe, tyr, trp)
 Termolisin  ile, leu, val
Analisis Rantai Ujung Peptida
 C terminal → carboxypeptidase
 N terminal → Sanger’s methode
Edmand degradation
 Sanger N-Terminal Analysis
- The N-terminal end of the polypeptide is labeled with 2,4-
dinitrofluorobenzene and the polypeptide is hydrolyzed
- The labeled N-terminal amino acid is separated from the
mixture and identified
 Edmand Degradation
- Edman degradation involve
sequential cleavage and
identification of N-terminal amino acids
- Edman degradation works well for
polypeptide sequence analyses up to
approximately 60 amino acid residues
 The N-terminal residue of the
polypeptide reacts with phenyl
isothiocyanate
 The resulting
phenylthiocarbamyl derivative is
cleaved from the peptide chain
 The unstable product rearranges
to a stable phenylthiohydantoin
(PTH) which is purified by HPLC
and identified by comparison
with PTH standards
Logika Penetapan Urutan
 Insulin merupakan peptida dg 30 asam amino. Mula2 dihidrolisis dg
sempurna, dianalisis dan diperoleh rumusnya:
Ala2ArgAsnCys2GlnGlu2Gly2His2Leu4LysPhe3ProSerThrTyr2Val3
Dg metode Sanger, diketahui bahwa asam amino ujung N adalah Phe,
sedangkan dg karboksipeptidase diketahui ujung C adl Ala. Dg
kimotripsin diperoleh 3 fragmen, 2 Phe, dan 1 Tyr. Setelah dipisahkan,
ketiga fragmen asam amino tersebut dianalisis dg degradasi Edman
diperoleh :
A. Leu-Val-Cys-Gly-Glu-Arg-Gly-Phe
B. Val-Asn-Gln-His-Leu-Cys-Gly-Ser-His-Leu-Val-Glu-Ala-Leu-Tyr
C. Thr-Pro-Lys-Ala
Dg tripsin diperoleh Ala, dan 2 peptida. Peptida yg lebih pendek dianalisis
dg metode Edman, diperoleh:
D. Gly-Phe-Phe-Tyr-Thr-Pro-Lys
 Dg logika maka dpt ditetapkan urutan insulin:
Phe-Val-Asn-Gln-His-Leu-Cys-Gly-Ser-His-Leu-Val-Glu-Ala-Leu-Tyr-Leu-
Val-Cys-Gly-Glu-Arg-Gly-Phe-Phe-Tyr-Thr-Pro-Lys-Ala
Latihan
1. Diberikan peptida dg urutan:
Ala-Gly-Tyr-Trp-Ser-Lys-Gly-Leu-Met-Gly
Tentukan fragmen yg terbentuk jk dihidrolisis dg:
a. Tripsin b. Kimotripsin c. Sianogen bromida

2. Bradikinin, suatu nonapeptida,


Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
Tentukan fragmen yg terbentuk jk dihidrolisis dg:
a. Tripsin b. Kimotripsin c. Pepsin
3. Suatu peptida dihidrolisis dengan enzim tripsin
menghasilkan fragmen
- Hys-Lys
- Trp-Arg
- Ala-Val-Phe-Gly-Lys
Dihidrolisis dengan enzim chymotrypsin dihasilkan
fragmen
- Gly-Lys-Trp
- Ala-Val-Phe
- Arg-Hys-Lys
Dari degradasi Edmand didapatkan residu Ala dan
hidrolisis carboxypeptidase didapatkan fragmen Lys.
Tuliskan rantai peptida yang dimaksud !
Sintesis Peptida
 Dg perlindungan ganda
R1 R1
perlindungan
asam amino H
H2N CH COOH P1 N CH COOH
aa1

R2 R2 O
perlindungan
karboksil
H2N CH COOH H2N CH C P2
aa2
R1 R2 O

H -H2O
P1 N CH COOH + H2N CH C P2

R1 O R2 O

H H
P1 N CH C N CH C P2
 Sintesis fase padat (solid phase synthesis)
CH2 CH2 CH2 CH2
CH CH CH CH

O O
CH2
H2NCHC NHCHCO
R' R
Protein
 Primary structure = the amino acid sequence
plus disulfide links
 Secondary structure = conformational

acids eg :  helix, pleated  sheet


relationship between nearest neighbor amino

 Tertiary structure : Refers to overall shape (how


the chain is folded) eg : Globular proteins
 Quaternary Structure : Some proteins are
assemblies of two or more chains. The way in
which these chains are organized is called the
quaternary structure.
Hemoglobin, for example, consists of 4 subunits

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