title: Determination of the composition, encapsulation efficiency and loading capacity in protein drug delivery systems using circular dichroism spectroscopy.
abstract: 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.
authors: Department of Chemistry, University of Miami, 1301 Memorial Drive, Coral Gables, FL 33146, United States.
authors: Zhili
authors: Z
authors: Peng
authors: Department of Chemistry, University of Miami, 1301 Memorial Drive, Coral Gables, FL 33146, United States.
authors: Shanghao
authors: S
authors: Li
authors: Department of Chemistry, University of Miami, 1301 Memorial Drive, Coral Gables, FL 33146, United States.
authors: Xu
authors: X
authors: Han
authors: Department of Chemistry, Faculty of Science, King Abdulaziz University, P.O. Box 80203, Jeddah 21589, Saudi Arabia.
authors: Abdulrahman O
authors: AO
authors: Al-Youbi
authors: Department of Chemistry, Faculty of Science, King Abdulaziz University, P.O. Box 80203, Jeddah 21589, Saudi Arabia.
authors: Abdulaziz S
authors: AS
authors: Bashammakh
authors: Department of Chemistry, Faculty of Science, King Abdulaziz University, P.O. Box 80203, Jeddah 21589, Saudi Arabia.
authors: Mohammad S
authors: MS
authors: El-Shahawi
authors: Department of Chemistry, University of Miami, 1301 Memorial Drive, Coral Gables, FL 33146, United States. Electronic address: rml@miami.edu.
authors: Roger M
authors: RM
authors: Leblanc
mesh_terms: D002942:Circular Dichroism; D016503:Drug Delivery Systems; D005916:Globulins / Q000737:chemistry*; D006454:Hemoglobins / Q000737:chemistry*; D006801:Humans; D012709:Serum Albumin / Q000737:chemistry*; D014168:Transferrin / Q000737:chemistry*; D000515:alpha 1-Antitrypsin / Q000737:chemistry*
chemical_list: D005916:Globulins; D006454:Hemoglobins; D012709:Serum Albumin; D014168:Transferrin; D000515:alpha 1-Antitrypsin
keywords: Circular dichroism spectroscopy; Drug delivery; Encapsulation efficiency; Loading capacity; Peptide and protein