TY - JOUR
T1 - Determination of the composition, encapsulation efficiency and loading capacity in protein drug delivery systems using circular dichroism spectroscopy
AU - Peng, Zhili
AU - Li, Shanghao
AU - Han, Xu
AU - Al-Youbi, Abdulrahman O.
AU - Bashammakh, Abdulaziz S.
AU - El-Shahawi, Mohammad S.
AU - Leblanc, Roger M.
N1 - Funding Information:
The authors gratefully acknowledge the support from King Abdulaziz University , Kingdom of Saudi Arabia, and University of Miami , USA.
Publisher Copyright:
© 2016 Elsevier B.V.
Copyright:
Copyright 2017 Elsevier B.V., All rights reserved.
PY - 2016/9/21
Y1 - 2016/9/21
N2 - Peptides and proteins have become very promising drug candidates in recent decades due to their unique properties. However, the application of these drugs has been limited by their high enzymatic susceptibility, low membrane permeability and poor bioavailability when administered orally. Considerable efforts have been made to design and develop drug delivery systems that could transport peptides and proteins to targeted area. Although it is of great importance to determine the composition after loading a drug to the carrier, the ability to do so is significantly limited by current analytical methods. In this letter, five important proteins, α1-antitrypsin, hemoglobin human, human serum albumin, human transferrin and r-globulin were chemically conjugated to two model drug carriers, namely carbon dots and polymer O-(2-carboxyethyl) polyethylene glycol. A simple yet convenient method based on circular dichroism spectroscopy was developed to determine the compositions of the various protein-carrier conjugates.
AB - Peptides and proteins have become very promising drug candidates in recent decades due to their unique properties. However, the application of these drugs has been limited by their high enzymatic susceptibility, low membrane permeability and poor bioavailability when administered orally. Considerable efforts have been made to design and develop drug delivery systems that could transport peptides and proteins to targeted area. Although it is of great importance to determine the composition after loading a drug to the carrier, the ability to do so is significantly limited by current analytical methods. In this letter, five important proteins, α1-antitrypsin, hemoglobin human, human serum albumin, human transferrin and r-globulin were chemically conjugated to two model drug carriers, namely carbon dots and polymer O-(2-carboxyethyl) polyethylene glycol. A simple yet convenient method based on circular dichroism spectroscopy was developed to determine the compositions of the various protein-carrier conjugates.
KW - Circular dichroism spectroscopy
KW - Drug delivery
KW - Encapsulation efficiency
KW - Loading capacity
KW - Peptide and protein
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U2 - 10.1016/j.aca.2016.08.014
DO - 10.1016/j.aca.2016.08.014
M3 - Article
C2 - 27590552
AN - SCOPUS:84989811858
VL - 937
SP - 113
EP - 118
JO - Analytica Chimica Acta
JF - Analytica Chimica Acta
SN - 0003-2670
ER -