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1956
DOI: 10.3181/00379727-91-22249
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Inhibition of Mumps and Influenza B Virus Multiplication by Synthetic Poly-D-Lysine.

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1957
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Cited by 9 publications
(2 citation statements)
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“…An 11‐residue model peptide, 2 , was used for these experiments, which was then modified via incorporation of d ‐lysine to tune the stability of the molecule. As we expected a 100 % d ‐amino acid containing peptide to be proteolytically stable, we investigated decreased percentages of d ‐amino acids to allow us to assess a range of stabilities from these diastereomeric peptides, as well as any protection from the fluorinated side‐chain.…”
Section: Figurementioning
confidence: 99%
“…An 11‐residue model peptide, 2 , was used for these experiments, which was then modified via incorporation of d ‐lysine to tune the stability of the molecule. As we expected a 100 % d ‐amino acid containing peptide to be proteolytically stable, we investigated decreased percentages of d ‐amino acids to allow us to assess a range of stabilities from these diastereomeric peptides, as well as any protection from the fluorinated side‐chain.…”
Section: Figurementioning
confidence: 99%
“…An 11-residue model peptide, 2,w as used for these experiments,w hich was then modified via incorporation of d-lysine to tune the stability of the molecule.Asweexpected a100 % d-amino acid containing peptide to be proteolytically stable, [24] we investigated decreased percentages of d-amino acids to allow us to assess ar ange of stabilities from these diastereomeric peptides,a s well as any protection from the fluorinated side-chain. To probe this,w es ubjected our lysine-rich peptides to trypsin to monitor the rate of degradation.…”
mentioning
confidence: 99%