Head-to-Tail Cyclization of α-Conotoxin TxID Leads to Enhanced Stability in Serum

Nurcan Biçen Karakoç; Muharrem Akcan

Makale detayları

Head-to-Tail Cyclization of α-Conotoxin TxID Leads to Enhanced Stability in Serum

Yazarlar:

Nurcan Biçen Karakoç | Muharrem Akcan

Yayıncı:

Gazi University

Ana Başlıklar:

Engineering

Dergi:

Gazi University Journal of Science Vol.37 Issue 2, pp.593-604

Belge Tipi:

Makale

Yayın Tarihi:

1/2024

Belge Dili:

İngilizce

Document ID (Org No.):

2001311654

pISSN:

2147-1762

Anahtar kelimeler:

Özet:

 Peptide biomolecules have important bioactivities and hence their use in drug design and development studies has increased in recent years. Conotoxins are natural peptides that obtained from cone snail venoms and have the potential to be used for chronic pain treatment, Parkinsons disease, schizophrenia, obesity and cancer due to their effects on the nervous system. However, their use as medicines has been limited as they can be easily broken down by many proteolytic enzymes in the body. Several modification methods are used to overcome these disadvantages. Cyclization of the peptide backbone is one such method and has been used to stabilize various linear peptides. In this study, the N- and C-termini of α-conotoxin TxID with two disulfide bridges were joined using a six amino acid long GGAAGG linker peptide chain to cyclize the peptide backbone and the serum stability of the cyclized peptide was examined. The cyclic TxID peptide remained intact about 50 in human serum after 24 hours.

 Peptide biomolecules have important bioactivities and hence their use in drug design and development studies has increased in recent years. Conotoxins are natural peptides that obtained from cone snail venoms and have the potential to be used for chronic pain treatment, Parkinsons disease, schizophrenia, obesity and cancer due to their effects on the nervous system. However, their use as medicines has been limited as they can be easily broken down by many proteolytic enzymes in the body. Several modification methods are used to overcome these disadvantages. Cyclization of the peptide backbone is one such method and has been used to stabilize various linear peptides. In this study, the N- and C-termini of α-conotoxin TxID with two disulfide bridges were joined using a six amino acid long GGAAGG linker peptide chain to cyclize the peptide backbone and the serum stability of the cyclized peptide was examined. The cyclic TxID peptide remained intact about 50 in human serum after 24 hours.

 Peptide biomolecules have important bioactivities and hence their use in drug design and development studies has increased in recent years. Conotoxins are natural peptides that obtained from cone snail venoms and have the potential to be used for chronic pain treatment, Parkinsons disease, schizophrenia, obesity and cancer due to their effects on the nervous system. However, their use as medicines has been limited as they can be easily broken down by many proteolytic enzymes in the body. Several modification methods are used to overcome these disadvantages. Cyclization of the peptide backbone is one such method and has been used to stabilize various linear peptides. In this study, the N- and C-termini of α-conotoxin TxID with two disulfide bridges were joined using a six amino acid long GGAAGG linker peptide chain to cyclize the peptide backbone and the serum stability of the cyclized peptide was examined. The cyclic TxID peptide remained intact about 50 in human serum after 24 hours.

 Peptide biomolecules have important bioactivities and hence their use in drug design and development studies has increased in recent years. Conotoxins are natural peptides that obtained from cone snail venoms and have the potential to be used for chronic pain treatment, Parkinsons disease, schizophrenia, obesity and cancer due to their effects on the nervous system. However, their use as medicines has been limited as they can be easily broken down by many proteolytic enzymes in the body. Several modification methods are used to overcome these disadvantages. Cyclization of the peptide backbone is one such method and has been used to stabilize various linear peptides. In this study, the N- and C-termini of α-conotoxin TxID with two disulfide bridges were joined using a six amino acid long GGAAGG linker peptide chain to cyclize the peptide backbone and the serum stability of the cyclized peptide was examined. The cyclic TxID peptide remained intact about 50 in human serum after 24 hours.

Makale detayları

Head-to-Tail Cyclization of α-Conotoxin TxID Leads to Enhanced Stability in Serum

Yazarlar:

Nurcan Biçen Karakoç | Muharrem Akcan

Yayıncı:

Gazi University

Ana Başlıklar:

Engineering

Dergi:

Gazi University Journal of Science Vol.37 Issue 2, pp.593-604

Belge Tipi:

Makale

Yayın Tarihi:

1/2024

Belge Dili:

İngilizce

Document ID (Org No.):

2001311654

pISSN:

2147-1762

Conotoxins

Peptide synthesis

Cyclization

Cyclic peptides

Serum stability

Sayı

Makale detayları

Head-to-Tail Cyclization of α-Conotoxin TxID Leads to Enhanced Stability in Serum

Yazarlar: Nurcan Biçen Karakoç | Muharrem Akcan

Yayıncı: Gazi University

Ana Başlıklar: Engineering

Dergi: Gazi University Journal of Science Vol.37 Issue 2, pp.593-604

Belge Tipi: Makale

Yayın Tarihi: 1/2024

Belge Dili: İngilizce

Document ID (Org No.): 2001311654

pISSN: 2147-1762

Conotoxins

Peptide synthesis

Cyclization

Cyclic peptides

Serum stability

Sayı

Yazarlar:

Nurcan Biçen Karakoç | Muharrem Akcan

Yayıncı:

Gazi University

Ana Başlıklar:

Engineering

Dergi:

Gazi University Journal of Science Vol.37 Issue 2, pp.593-604

Belge Tipi:

Makale

Yayın Tarihi:

1/2024

Belge Dili:

İngilizce

Document ID (Org No.):

2001311654

pISSN:

2147-1762