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Chapter: Pharmaceutical Drugs and Dosage: Protein and peptide drug delivery

Pharmaceutical Drugs and Dosage: Protein and peptide drug delivery - Review questions answers


Review questions

25.1 Most protein drugs have poor oral absorption because of their

A.      Large molecular size and high hydrophilicity

B.      Poor transport via the paracellular route

C.      Negligible passive diffusion

D.      Degradation in the GI tract

E.       All of the above

25.2 Protein aggregation in an oral solution formulation can be mini-mized by

A.      Conjugation to PEG

B.      pH optimization

C.      Addition of certain polymers

D.      Addition of sugars to the formulation

E.       All of the above

25.3 Which of the following enzymes is most responsible for protein metabolism and degradation?

A.      Proteases

B.      Kinases

C.      Oxidases

D.      Phosphorylases

25.4 Which of the following antioxidant is not a metal chelator?

A.      EDTA

B.      EGTA

C.      DTPA

D.      Ascorbic acid

E.       Citric acid

25.5 Which of the following level of protein structure is only possible for proteins that have more than one polypeptide chain?

A.      Primary structure

B.      Secondary structure

C.      Tertiary structure

D.      Quaternary structure

E.       All of the above

25.6 Which of the following antibody is expected to be least antigenic and immunogenic?

A.      Antihuman CD31 mouse monoclonal antibody

B.      Antihuman CD31 humanized mouse monoclonal antibody

C.      Antihuman CD31 human monoclonal antibody

D.      Antihuman CD31 mouse domain antibody

E.       Antihuman CD31 mouse-human chimeric monoclonal antibody

25.7 Aqueous protein solubility is least likely to depend on

A.      pH

B.      Salt concentration

C.      Isoelectric point

D.      Cosolvent content

E.       Preservative content

25.8 Which of the following does not represent an advantage of lyophilization?

A.      Improving chemical stability of the protein

B.      Ease of handling and transportation

C.      Economically cheaper option of protein formulation

D.      Reducing the kinetics of degradation reactions

25.9 Which of the following amino acid residues are sensitive to deamida-tion? Select all that apply.

A.      Asparagine

B.      Cysteine

C.      Glutamine

D.      Histidine

E.       Proline

25.10 Which of the following amino acid residues are sensitive to disulfide exchange? Select all that apply.

A.      Asparagine

B.      Cysteine

C.      Glutamine

D.      Histidine

E.       Proline

25.11  Which of the following amino acid residues are sensitive to oxida-tion? Select all that apply.

A.      Asparagine

B.      Cysteine

C.      Glutamine

D.      Histidine

E.       Proline

25.12 Which statements are TRUE and which ones are FALSE?

A.      The secondary structure of proteins refers to the conformation of the polypeptide backbone.

B.      Oxidation of methionine to methionine sulfoxide can be reversed with a suitable reducing agent.

C.      The peptide bond between aspartic acid and proline are suscep-tible to hydrolysis at acidic pH.

D.      The amide groups of asparaginyl and glutaminyl residues are labile at acidic pH.

E.       High residual moisture content may induce aggregation of the lyophilized proteins.

F.       Exposure to hydrophobic surfaces may promote protein aggregation.

25.13 Protein denaturation

A.      Can be either reversible or irreversible

B.      Can be caused by exposure to hydrophobic surfaces

C.      Can be induced extreme pH

D.      All of the above

25.14 Name three functional groups in proteins, which can be used for conjugation.

25.15 Why to PEGylate protein drugs? How will you PEGylate insulin?

Answers:

25.1 E.

25.2 E.

25.3 A.

25.4 D.

25.5 D.

25.6 C.

25.7 E.

25.8 C.

25.9 A and C.

25.10 B.

25.11 B and D

25.12 A.True

B. True

C. True

D. True

E. True

F. True

25.13 D.

25.14 Amino groups of N-terminal amino acid or ε-amino groups of lysine (–NH2), carboxyl group of aspartic and glutamic acids (–COOH), and sulfhydryl group of cysteine (–SH).

25.15 Proteins are often conjugated to polyethylene glycol (PEG), which is nonimmunogenic and nontoxic. In protein molecules, N-hydroxysuccinimide (NHS) ester groups primarily react with the α-amines at the N-terminals and the ε-amines of lysine side chains. PEGylation can provide increased biocompatibility, reduce immune response, increase in vivo stability, delayed clearance by the reticuloendothelial system, and prevent protein adsorption on the surface.

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