ScienceGuardians

ScienceGuardians

Did You Know?

ScienceGuardians gives voice to all stakeholders

Molecular characterization, antibacterial and immunoregulatory activities of liver-expressed antimicrobial peptide 2 in black rockfish, Sebastes schlegelii

Authors: Min Zhang,Xue Yan,Chang-biao Wang,Wen-qing Liu,Yue Wang,Hao Jing,Bing Wang,Kai Yang,Zi-yue Chen,Yu-yu Luan,Guang-hua Wang
Journal: Fish
Publisher: Elsevier BV
Publish date: 2024-4
ISSN: 1050-4648 DOI: 10.1016/j.fsi.2024.109467
View on Publisher's Website
Up
0
Down
::

On Page 6, under Section 3.1: Molecular characterization of SsLEAP2, the authors state:

“SsLEAP2 contains a signal peptide sequence (position 1–29), a prodomain (position 30–53) and a mature peptide (position 54–99) (Fig. 1), in which four cysteine residues forming three disulfide bonds (Cys70 – Cys81, Cys76 – Cys86).”

This is scientifically impossible.

Four cysteine residues can form a maximum of two disulfide bonds, not three.

The statement “four cysteine residues forming three disulfide bonds” is chemically incorrect and reflects a fundamental misunderstanding of protein biochemistry.

  • You must be logged in to reply to this topic.