Search

Hemoglobin A1c (HbA1c) is a long-term measure for glucose concentration in plasma. Since its introduction as a diabetes monitoring tool, and its more recent application as a diagnostic tool, the number of measurements of HbA1c have risen dramatically. However, HbA1c change is slow, so repeating measurements should not be done too often. We use a large, unfiltered dataset from 52,017 patients to determine the possible rate of change in HbA1c concentration. In our laboratory, the critical difference between HbA1c measurements is 8.5%. Our data show that a 1-unit HbA1c rise takes 4 weeks to occur, hence, at a HbA1c concentration around 50 mmol/mol Hgb, a critically increased HbA1c concentration cannot be determined until after 16 weeks. Conversely a critically lower HbA1c can manifest itself after 2 weeks, but after 7 weeks the dropping tendency stops. The amount of measurements that can be cancelled because they were taken sooner than 16 weeks is 23 percent. [ABSTRACT FROM AUTHOR]

Hemoglobin A 1c (HbA 1c ) is a long-term measure for glucose concentration in plasma. Since its introduction as a diabetes monitoring tool, and its more recent application as a diagnostic tool, the number of measurements of HbA 1c have risen dramatically. However, HbA 1c change is slow, so repeating measurements should not be done too often. We use a large, unfiltered dataset from 52,017 patients to determine the possible rate of change in HbA 1c concentration. In our laboratory, the critical difference between HbA 1c measurements is 8.5%. Our data show that a 1-unit HbA 1c rise takes 4 weeks to occur, hence, at a HbA 1c concentration around 50 mmol/mol Hgb, a critically increased HbA 1c concentration cannot be determined until after 16 weeks. Conversely a critically lower HbA1c can manifest itself after 2 weeks, but after 7 weeks the dropping tendency stops. The amount of measurements that can be cancelled because they were taken sooner than 16 weeks is 23 percent.

Peptoids (N-substituted glycines) are mimics of α-peptides in which the side chains are attached to the backbone N (α) -amide nitrogen instead of the C (α) -atom. Peptoids hold promise as therapeutics since they often retain the biological activity of the parent peptide and are stable to proteases. In recent years, peptoids have attracted attention as new potential antibiotics against multiresistant bacteria. Here we describe the submonomer solid-phase synthesis of an antimicrobial peptoid, H-Nmbn-Nlys-Nlys-Nnap-Nbut-Nmbn-Nlys-NH2.