Inherent to the design of this synthesis was a desire to probe the SAR of the lysine residue as crystallographic studies indicate the importance of this side chain as indicated by its interactions with the phosphate moieties of lipids. The ability to access a library of analogs requires late-stage homologation to arrive at 1. Thus, installation of a cyano group followed by reduction provided the desired side chain through a simple four step sequence: (a) methanolysis of 23 to 24 (76% yield), (b) mesylation and concomitant TES deprotection in the presence of methanesulfonic acid, (c) cyanation under phase transfer conditions, and (d) reduction of both the nitrile and AQ ring with in situ generated nickel boride followed by in situ Boc protection. The fortuitous reduction of the AQ allowed for its smooth removal using conditions developed by Geyer 44 (as inspired by methodology from the Dawson group). Consequently, treatment of 25 with triphosgene followed by hydrolysis with trimethyltin hydroxide delivered 26 in 33% yield over 5 steps. With the carboxylic acid revealed, conditions were evaluated to install the side chain 27 (synthesized from 5 and 8, see SI). Numerous peptide coupling reagents were screened for this transformation, however successful amide bond formation was only observed in appreciable quantities using a combination of EDCI and HOAt. The product of the coupling reaction was then subjected to ammonolysis to convert the aspartate residue to the asparagine 28. At this stage, all that remained was global deprotection, which was realized by treatment of 28 with a combination of TMSOTf, TFA, thioanisole, and ethane dithiol to complete the synthesis of 1 in 14% yield for the final sequence (18 steps LLS from 15).