Colleagues are mourning the loss of David Allsop, a pioneer in Alzheimer's research. Allsop passed away March 8 after a battle with cancer. He was 67. An Alzforum member and contributor, Allsop co-chaired, with Ashley Bush, one of our early webinars on the role of metals in amyloid fibril toxicity. “Although somewhat shy, David was a man of many firsts. He was widely respected for his many contributions to AD and protein aggregation research,” wrote Dominic Walsh, Brigham and Women’s Hospital, Boston. Allsop and Walsh were collaborators.   

David Allsop (left) and Dominic Walsh on the quad at Harvard Medical School, December 2017.

Allsop had a varied career, working in both academia and industry. In his early days, while working with Michael Kidd at the University of Nottingham, U.K., he isolated plaque cores from human AD brains. He determined their amino acid composition, which would later turn out to be spot-on with the amyloid-β sequence (Allsop et al., 1983). Allsop was the first to raise monoclonal antibodies to that peptide, and he showed that they reacted with plaque cores and cerebral amyloid angiopathy, but not with neurofibrillary tangles (Allsop et al., 1988). This helped settle a major debate at the time, about whether plaques and tangles were related.

Allsop continued to study plaques, in both AD and Down’s syndrome, when he worked with George Glenner at the University of California, San Diego. His 1990 review, together with John Hardy, then at St. Mary’s Hospital, London, on amyloid deposition as a central event in AD has been cited more than 600 times (Hardy and Allsop, 1991). 

At CTAD, 2017.

Allsop spent two years working on AD in Japan, where he became assistant director of what was then the Psychiatric Research Institute of Tokyo, now part of the Tokyo Metropolitan Institute of Medical Science. Together with Tsuyoshi Ishii and colleagues, he found evidence for an amyloid precursor protein secretase in rat brain (Allsop et al., 1991). He subsequently joined the faculty at Queen’s University, Belfast, and worked in industry for a brief period, at SmithKline Beecham. He ultimately became chair of the department of neuroscience at Lancaster University, where he worked until his death.

Allsop was fascinated by the role of metals in fibril toxicity and by what could be learned from biological fluid markers. The first report of α-synuclein in cerebrospinal fluid came from his lab (El-Agnaf et al., 2003). More recently, Allsop became interested in the role of pollutants in dementia (Tabner et al., 2010; Mayes et al., 2014; Maher et al., 2016). 

“He was someone to have a beer with, swap a bit of gossip with, as well as swap ideas,” wrote Hardy, now at University College London, and Eric Karran, who worked with Allsop at SmithKline Beecham. “He did not get the recognition he deserved, but I am sure that did not bother him. He just liked scientific experiments and generating and interpreting data. We’ll both miss him.” See tributes below.—Tom Fagan


  1. David Allsop was a seminal figure in Alzheimer’s research, and his death at such an early age is a great loss. He was a friend and colleague of us both.

    Beneath a slightly shambling and bear-like exterior with an easygoing manner, David had a sharp mind and passion for detail. In 1983, when at Nottingham University, he published the first amino acid composition of plaque cores. This was clearly a breakthrough, because plaque separation was extremely problematic. Years later, Konrad Beyreuther commented publicly that he and Colin Masters had expected the Nottingham group to publish the amyloid sequence and then to clone the APP gene … but their MRC grant renewal was not funded, and this stopped their progress. When we (JH) identified APP mutations in 1990, it told us that amyloid was important, but not why it was important, so I (JH) phoned up Dave and we wrote the well-cited review together. Because of the funding issues alluded to, Dave decided to move to (then) SmithKline Beecham. In many ways, this was a surprise, as Dave was really the classic academic and not at all a company man. 

    One famous incident that Dave provoked was at the first Alzheimer's congress in Padua, Italy. The plenary lecture was on APP processing, and Dave was in the audience. Despite his thick spectacles and casual air, when he was interested in something, he really paid extremely close attention to data and, at the end of the presentation, Dave stood up and said, “Can you go back to slide 14 please?” And then, “I think you have misinterpreted your data. Just compare that blot with the one in slide 17.” At this point, the lecturer was clearly getting tense. And then David said, “Yes … You have got this wrong.” A hush fell over the audience and Dave was oblivious to the rising tension in the hall. The lecturer said something that was not for attribution, and the chair quickly closed the session. I strongly suspect that Dave was correct … For him it was only about the data.

    I (EK) got to know David well when he became my boss at SmithKline Beecham. In a way, this was a surprising move, as John points out. I remember Dave would sit at his desk and read papers by running a ruler down them, line by line, and then meticulously underline the points he thought were important. I also well recall having a discussion about Aβ (what else?) and Dave wrote out the 42 amino acid sequence from memory ... which was astonishing to me. While Dave would appear to be laid-back, once he got an idea, he would look into the middle distance, and lay it out in a manner that brooked no interruption. David did a postdoc in Japan, and took his family with him. His children were young at this time. I asked Dave how they had got on, and he told me that he had put them into a Japanese school—which would, I think, have terrified most parents. Dave nonchalantly told me that, “They were a bit confused for the first three months, but after that they came home and started speaking Japanese.” I learnt a lot from David about Alzheimer’s disease, and when we were at meetings together, he was always being asked his opinion from a broad swathe of the scientific community. I memorably introduced Dave to the dry martini at a party at my house. He greatly enjoyed his first. By his second, he was starting to forget that when he was drinking, he shouldn't try to talk, and when he was talking, he shouldn’t try to drink. He knew how to enjoy himself!

    For both of us, seeing Dave, often in the company of Dave Mann at Alzheimer’s meetings, was always a pleasure. He was someone to have a beer with, swap a bit of gossip with, as well as swap ideas. He did not get the recognition he deserved, but I am sure that did not bother him. He just liked scientific experiments and generating and interpreting data. We’ll both miss him.

  2. David Allsop was a man of several important firsts and was widely respected for his many contributions to AD research. In the early 1980s, David worked at the University of Nottingham, where, with Michael Kidd, the discoverer of neurofibrillary tangles, he isolated amyloid plaques from AD brain and elucidated their amino acid composition. He later moved to San Diego, where he worked with George Glenner and developed the first anti-Aβ monoclonal antibodies and provided biochemical evidence that Aβ is derived from APP.

    It was in San Diego that David struck up a series of collaborations with Japanese colleagues, which led to him joining the Tokyo Psychiatric Research Institute, where he was assistant director. After two years in Japan, David returned to Europe to establish a laboratory at Queen’s University, Belfast, and penned his highly influential review with John Hardy, “Amyloid deposition as the central event in the aetiology of Alzheimer's disease.” In 1994 David joined SmithKline Beecham, supporting the team that subsequently co-discovered BACE. He returned to academia in 1998, when he joined Lancaster University and was appointed chair in neuroscience in 2002. During his tenure at Lancaster, David developed a large, well-funded research group, covering topics as diverse as the first report that α-synuclein is present in blood and CSF, and intriguing data linking air pollution to AD.

    I had the honor to work with David between 1992 and 1994, and we became fast friends. He was a fantastic human being, and a wonderful scientist. David had a hugely positive influence on me and on many other young scientists. I well remember him telling me, “Being first is nice, but being right is much more important. We have the privilege to do fascinating and stimulating research, but we work on a dreadful disease, and we have a weighty obligation to the patients we serve.” These words so impressed me that I have felt compelled to share them with the students and postdocs who have worked with me.

    David could be a little shy, but once he got to know people, he was very talkative. He was super enthusiastic about everything, especially science. Students loved David. In the early 1990s when Alzheimer’s disease was not so widely recognized, the undergrads at Queen’s often referred to Alzheimer’s as “Allsoper’s disease.” David was a fully rounded individual. He was a talented guitarist and played in several bands. But most of all David loved his wife and family, and they were a source of great pride and joy.

    I suspect anyone who knew David smiles at the mention of his name. He was positive, kind, generous, and a bundle of fun.

    I thank God for the blessing of having worked with and known David Allsop.


    . Amyloid deposition as the central event in the aetiology of Alzheimer's disease. Trends Pharmacol Sci. 1991 Oct;12(10):383-8. PubMed.

  3. David, of course, was best known for his interest in amyloid. Later in his career he became interested in magnetite (iron oxide) nanoparticles within amyloid. This was great, detailed work with huge implications for the role of pollution in exacerbating Alzheimer’s disease.

    He was always a gentleman in exchanges and a very likeable and serious scientist.

    He is a great loss to the British Alzheimer’s research community.

    Vale, David.

  4. David Allsop (1954- 2021)

    David Allsop was a pioneer in the modern era of Alzheimer’s disease molecular pathogenesis. Mentored by Michael Landon (biochemist) and Michael Kidd (human morphologist, electron microscopist) at the Queen’s Medical Centre, University of Nottingham, they succeeded in determining the amino acid composition of purified amyloid plaque cores (APC) from the Alzheimer’s disease (AD) brain (Allsop et al., 1983). Most people at the time of this publication, and even today, some 40 years later, do not appreciate the significance of this data. Knowing the amino acid composition of the APC was essential for determining the C-terminus of Aβ, based on our studies of the c-DNA sequence of APP and the cyanogen-bromide cleavage fractions of APC (Kang et al., 1987). Yes, we knew the amino acid composition of APC based on our own and subsequent studies. Yes, we can debate whether they were the first to isolate native APC compared to our work (Merz et al., 1983). Yes, they didn’t figure out how to solubilize the APC and get Aβ to run on an SDS- PAGE gel and thereby determine its subunit size. None of this detracts from their discovery of the amino acid composition of APC.

    Looking back at Allsop et al.’s 1983 publication, it is so nice to see who they referenced: the doyens of classical amyloidology: Earl Benditt, Merrill Benson, Per Westermark, M. Dalakis, King Engel, Alan Cohen, Martha Skinner, Gunnar Husby, Knut Sletten, J.B. Natvig, G.D. Sorenson, and George Glenner, who all need to be recognized as the founders on whose shoulders we stand.

    Allsop’s second publication was a brief letter to The Lancet (Kidd et al., 1985) drawing attention to Divry’s 1927 description of the APC. Glenner’s β-protein paper did not reference their APC amino acid composition, nor Ihara, Abraham, and Selkoe’s paper on the amino acid composition data of paired helical filament (PHF) preparations. They suggested that the PHF and APC subunit may be identical, an issue that remains unresolved, even in today’s cryo-electron microscopy world.

    Allsop then published an interesting paper in 1986, in which the first use of the term “amorphous” plaques was introduced in relation to APC in Down’s Syndrome (Allsop et al., 1986). This concept remains a hot issue as we move into an era of anti-Aβ therapeutics, in which Aβ-PET signals are reduced, but we remain uncertain as to whether the PET signals are reporting on APC or “amorphous” plaques.

    Also in 1986, Allsop published the first monoclonal antibody to the N-terminus of synthetic Aβ 8-17 (Allsop et al., 1986). Yes, others had polyclonals to APC and synthetic peptides of Aβ, but today, we should celebrate that this development had paved the way toward the first disease modifying therapy for AD.

    We salute and pay tribute to David Allsop’s contributions to the AD saga.


    . The isolation and amino acid composition of senile plaque core protein. Brain Res. 1983 Jan 24;259(2):348-52. PubMed.

    . The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor. Nature. 1987 Feb 19-25;325(6106):733-6. PubMed.

    . Ultrastructural morphology of amyloid fibrils from neuritic and amyloid plaques. Acta Neuropathol. 1983;60(1-2):113-24. PubMed.

    . Senile plaque amyloid, paired helical filaments, and cerebrovascular amyloid in Alzheimer's disease are all deposits of the same protein. Lancet. 1985 Feb 2;1(8423):278. PubMed.

    . Isolated senile plaque cores in Alzheimer's disease and Down's syndrome show differences in morphology. J Neurol Neurosurg Psychiatry. 1986 Aug;49(8):886-92. PubMed.

    . Monoclonal antibodies raised against a subsequence of senile plaque core protein react with plaque cores, plaque periphery and cerebrovascular amyloid in Alzheimer's disease. Neurosci Lett. 1986 Jul 24;68(2):252-6. PubMed.

  5. David was so supportive to me when I first started my own group here in St. Andrews over 20 years ago. As the other comments have said, he was such a gentleman and was very encouraging when we first started into our more chemistry-guided approach to studying Alzheimer's disease. From having sat on many funding councils, I can tell you David's ideas were always imaginative and pioneering, and I admit, shaped many of what we do in the lab still. He will be missed.

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Webinar Citations

  1. Role and Control of Metal-Mediated Fibril Toxicity

Paper Citations

  1. . The isolation and amino acid composition of senile plaque core protein. Brain Res. 1983 Jan 24;259(2):348-52. PubMed.
  2. . Immunohistochemical evidence for the derivation of a peptide ligand from the amyloid beta-protein precursor of Alzheimer disease. Proc Natl Acad Sci U S A. 1988 Apr;85(8):2790-4. PubMed.
  3. . Amyloid deposition as the central event in the aetiology of Alzheimer's disease. Trends Pharmacol Sci. 1991 Oct;12(10):383-8. PubMed.
  4. . Alzheimer amyloid beta/A4 peptide binding sites and a possible 'APP-secretase' activity associated with rat brain cortical membranes. Brain Res. 1991 Jun 14;551(1-2):1-9. PubMed.
  5. . Alpha-synuclein implicated in Parkinson's disease is present in extracellular biological fluids, including human plasma. FASEB J. 2003 Oct;17(13):1945-7. PubMed.
  6. . Hypothesis: soluble aβ oligomers in association with redox-active metal ions are the optimal generators of reactive oxygen species in Alzheimer's disease. Int J Alzheimers Dis. 2010;2011:546380. PubMed.
  7. . β-amyloid fibrils in Alzheimer disease are not inert when bound to copper ions but can degrade hydrogen peroxide and generate reactive oxygen species. J Biol Chem. 2014 Apr 25;289(17):12052-62. Epub 2014 Mar 11 PubMed.
  8. . Magnetite pollution nanoparticles in the human brain. Proc Natl Acad Sci U S A. 2016 Sep 27;113(39):10797-801. Epub 2016 Sep 6 PubMed.

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