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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