Managing hundreds of improvement teams.

Recognizing the notable scale of USAID Applying Science to Strengthen and Improve Systems (ASSIST) Project activities and sizable number of improvement teams, which in some cases is close to 1,000 improvement teams managed in one country at a point in time, we sought to answer the questions: How do we manage hundreds of improvement teams in one country alone? How do we manage more than 4,000 improvement teams globally? The leaders of our improvement programs manage such efforts as though they are second-nature, without pointing to the specific skills and strategies needed to manage thousands of teams. This paper was developed to capture the lessons, considerations, and insights shared in discussions with leaders on the USAID ASSIST Project, including country Chiefs of Party and Regional Directors. More specifically, this paper seeks to describe what is involved in scaling up and managing large numbers of improvement teams.

Unpacking the black box of improvement.

During the Salzburg Global Seminar Session 565-'Better Health Care: How do we learn about improvement?', participants discussed the need to unpack the 'black box' of improvement. The 'black box' refers to the fact that when quality improvement interventions are described or evaluated, there is a tendency to assume a simple, linear path between the intervention and the outcomes it yields. It is also assumed that it is enough to evaluate the results without understanding the process of by which the improvement took place.

Effect of peptide conformation on membrane permeability.

The effect of peptide conformational constraint on the peptide permeation across the model membranes was examined by determining the permeability of pairs of cyclic and acyclic peptides related to c[d-Pen2, d-Pen5] enkephalin (DPDPE). The peptides were cyclized by formation of an intramolecular disulfide bridge between the second and fifth residues composed of either d-penicillamine or cysteine. In each case the acyclic peptide was three to seven times more permeable than corresponding cyclic peptide.

Glycopeptide-membrane interactions: glycosyl enkephalin analogues adopt turn conformations by NMR and CD in amphipathic media.

Four enkephalin analogues (Tyr-D-Thr-Gly-Phe-Leu-Ser-CONH(2), 1, and the related O-linked glycopeptides bearing the monosaccharide beta-glucose, 2, the disaccharide beta-maltose, 3, and the trisaccharide beta-maltotriose, 4) were synthesized, purified by HPLC, and biophysical studies were conducted to examine their interactions with membrane model systems. Glycopeptide 2 has been previously reported to penetrate the blood-brain barrier (BBB), and produce potent analgesia superior to morphine in mice (J. Med.

Myristoylated alanine-rich C kinase substrate (MARCKS) produces reversible inhibition of phospholipase C by sequestering phosphatidylinositol 4,5-bisphosphate in lateral domains.

The myristoylated alanine-rich protein kinase C substrate (MARCKS) is a major protein kinase C (PKC) substrate in many different cell types. MARCKS is bound to the plasma membrane, and several recent studies suggest that this binding requires both hydrophobic insertion of its myristate chain into the bilayer and electrostatic interaction of its cluster of basic residues with acidic lipids. Phosphorylation of MARCKS by PKC introduces negative charges into the basic cluster, reducing its electrostatic interaction with acidic lipids and producing translocation of MARCKS from membrane to cytoplasm.