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Hydroxy fatty acids (HFAs) have found wide use in today's market, ranging from industrial materials to pharmaceuticals. Castor oil, which is obtained from castor seeds, has served as a primary source of the most common HFA, ricinoleic acid, but also contains several undesirable compounds which pose severe health risks, the most notable being ricin, an unusually stable, toxic protein. A promising HFA alternative is lesquerella oil, an oil obtained from seeds of the Lesquerella fendleri species. Lesquerella oil is mainly comprised of lesquerolic acid, an HFA that is structurally similar to ricinoleic acid, the only difference being that lesquerolic acid possesses two additional methylene groups on the carboxyl end of the molecule. In addition, the bisphosphonate moiety has been shown to display interesting biological activities, primarily as osteoporosis drugs and anti‐cancer therapeutics. The synthesis of lesquerella‐based bisphosphonates, both an unsaturated and saturated series, have been produced in high yields and high purity and are reported here. [ABSTRACT FROM AUTHOR]

Hydroxy fatty acids (HFAs) have long been a staple component of feedstock oils with uses ranging from motor oils to food to pharmaceuticals. Castor oil, which contains the HFA ricinoleic acid as its principal component, is the most widely used source of HFA in the world. In addition, bisphosphonates are a functional moiety that has been shown to display a variety of industrial applications, ranging from use in water softeners to osteoporosis drugs, primarily due to their affinity for the calcium ion. We have long been interested in the modification of ricinoleic acid from castor oil to phosphorus derivatives, including α‐hydroxy phosphonates and phosphonic acids, and have now accomplished the synthesis of a family of ricinoleic‐derived bisphosphonates: one that retains the cis alkene found in ricinoleic acid and one where the alkene has undergone hydrogenation. These compounds have been produced in high yields and high purity and the synthesis of these compounds is reported. [ABSTRACT FROM AUTHOR]

Herein we describe a synthetically simple strategy for increasing the lifetime of unstructured peptides in cytosolic environment via dimerization at the N-terminus to block threading into the catalytic cleft of cytosolic proteases. We establish this approach with kinase substrates, allowing for phosphorylation in cells as a demonstration of protease resistance.