Discovery of potential carbonic anhydrase I and II inhibitors: D-Penicillamine derivatives

Işıl Nihan Korkmaz

Makale detayları

Discovery of potential carbonic anhydrase I and II inhibitors: D-Penicillamine derivatives

Yazarlar:

Işıl Nihan Korkmaz

Yayıncı:

Gumushane University

Ana Başlıklar:

Enzimler

Dergi:

Gümüşhane Üniversitesi Fen Bilimleri Dergisi Vol.14 Issue 1, pp.274-282

Belge Tipi:

Makale

Yayın Tarihi:

3/2024

Belge Dili:

Türkçe

Document ID (Org No.):

2001313136

pISSN:

2146-538X

Anahtar kelimeler:

Özet:

 Penicillamine, an amino acid derivative that does not participate in the protein structure, is a trifunctional organic molecule composed of a carboxylic acid, a thiol, and an amine. D-Penicillamine PEN-1, N-Acetyl-D-Penicillamine PEN-2 and D Penicillamine disulfide PEN-3, which are used in the treatment of many diseases, especially Wilsons disease, are produced by carbonic anhydrase I and II hCA I in vitro. Inhibition effects on hCA II isoenzymes were investigated. hCA I, hCA II enzymes were isolated from human erythrocyte cells. It was determined that PEN-1, PEN-2, and PEN-3 effectively inhibited both purified enzymes. The IC50 values of PEN-1, PEN-2, and PEN-3 molecules were calculated to be 387.21, 407.49, and 106.75 µM for hCA I, 563.72 364.87, and 136.91 µM for hCA II, respectively. The inhibition type for all molecules was determined as competitive inhibition in both enzymes.

 Penicillamine, an amino acid derivative that does not participate in the protein structure, is a trifunctional organic molecule composed of a carboxylic acid, a thiol, and an amine. D-Penicillamine PEN-1, N-Acetyl-D-Penicillamine PEN-2 and D Penicillamine disulfide PEN-3, which are used in the treatment of many diseases, especially Wilsons disease, are produced by carbonic anhydrase I and II hCA I in vitro. Inhibition effects on hCA II isoenzymes were investigated. hCA I, hCA II enzymes were isolated from human erythrocyte cells. It was determined that PEN-1, PEN-2, and PEN-3 effectively inhibited both purified enzymes. The IC50 values of PEN-1, PEN-2, and PEN-3 molecules were calculated to be 387.21, 407.49, and 106.75 µM for hCA I, 563.72 364.87, and 136.91 µM for hCA II, respectively. The inhibition type for all molecules was determined as competitive inhibition in both enzymes.

 Penicillamine, an amino acid derivative that does not participate in the protein structure, is a trifunctional organic molecule composed of a carboxylic acid, a thiol, and an amine. D-Penicillamine PEN-1, N-Acetyl-D-Penicillamine PEN-2 and D Penicillamine disulfide PEN-3, which are used in the treatment of many diseases, especially Wilsons disease, are produced by carbonic anhydrase I and II hCA I in vitro. Inhibition effects on hCA II isoenzymes were investigated. hCA I, hCA II enzymes were isolated from human erythrocyte cells. It was determined that PEN-1, PEN-2, and PEN-3 effectively inhibited both purified enzymes. The IC50 values of PEN-1, PEN-2, and PEN-3 molecules were calculated to be 387.21, 407.49, and 106.75 µM for hCA I, 563.72 364.87, and 136.91 µM for hCA II, respectively. The inhibition type for all molecules was determined as competitive inhibition in both enzymes.

 Protein yapısına katılmayan bir aminoasit türevi olan penisilamin; bir karboksilik asit, bir tiyol ve aminden oluşan üç işlevli bir organik moleküldür. Başta Wilson hastalığı olmak üzere birçok hastalığın tedavisinde kullanılan D-Penisilamin PEN-1, N-Asetil-D-Penisilamin PEN-2 ve D-Penisilamin disülfit PEN-3 in vitro koşullarda karbonik anhidraz I ve II hCA I, hCA II izoezimleri üzerindeki inhibisyon etkileri araştırıldı. İnsan eritrosit hücrelerinden hCA I, hCA II enzimleri izole edildi. Saflaştırılan her iki enzimin D-Penisilamin ve türevleri tarafından etkili bir şekilde inhibe edildiği belirlendi. PEN-1, PEN-2 ve PEN-3 moleküllerinin IC50 değerleri hCA I için sırasıyla 387.21; 407.49 ve 106.75 µM, hCA II için sırasıyla 563.72; 364.87 ve 136.91 µM olarak hesaplandı. Bütün moleküller için inhibisyon tipi her iki enzimde de yarışmalı inhibisyon olarak belirlendi.

Makale detayları

Discovery of potential carbonic anhydrase I and II inhibitors: D-Penicillamine derivatives

Yazarlar:

Işıl Nihan Korkmaz

Yayıncı:

Gumushane University

Ana Başlıklar:

Enzimler

Dergi:

Gümüşhane Üniversitesi Fen Bilimleri Dergisi Vol.14 Issue 1, pp.274-282

Belge Tipi:

Makale

Yayın Tarihi:

3/2024

Belge Dili:

Türkçe

Document ID (Org No.):

2001313136

pISSN:

2146-538X

Affinity chromatography

Inhibition

Carbonic anhydrase

PenicillamineAfinite kromatografisi

İnhibisyon

Karbonik anhidraz

Penisilamin

Sayı

Makale detayları

Yazarlar: Işıl Nihan Korkmaz

Yayıncı: Gumushane University

Ana Başlıklar: Enzimler

Dergi: Gümüşhane Üniversitesi Fen Bilimleri Dergisi Vol.14 Issue 1, pp.274-282

Belge Tipi: Makale

Yayın Tarihi: 3/2024

Belge Dili: Türkçe

Document ID (Org No.): 2001313136

pISSN: 2146-538X

Sayı

Yazarlar:

Işıl Nihan Korkmaz

Yayıncı:

Gumushane University

Ana Başlıklar:

Enzimler

Dergi:

Gümüşhane Üniversitesi Fen Bilimleri Dergisi Vol.14 Issue 1, pp.274-282

Belge Tipi:

Makale

Yayın Tarihi:

3/2024

Belge Dili:

Türkçe

Document ID (Org No.):

2001313136

pISSN:

2146-538X